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PDBsum entry 2xok

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2xok
Jmol
Contents
Protein chains
483 a.a. *
471 a.a. *
266 a.a. *
119 a.a. *
49 a.a. *
(+ 4 more) 73 a.a. *
Ligands
ANP ×5
Metals
_MG ×5
* Residue conservation analysis
PDB id:
2xok
Name: Hydrolase
Title: Refined structure of yeast f1c10 atpase complex to 3 a resolution
Structure: Atp synthase subunit alpha, mitochondrial. Chain: a, b, c. Atp synthase subunit beta, mitochondrial. Chain: d, e, f. Atp synthase subunit gamma, mitochondrial. Chain: g. Synonym: f-atpase gamma subunit. Atp synthase. Chain: h.
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Organelle: mitochondrion. Other_details: mitochondrion. Organelle: mitochondrion
Resolution:
3.01Å     R-factor:   0.210     R-free:   0.253
Authors: D.Stock,A.G.W Leslie,J.E.Walker
Key ref:
D.Stock et al. (1999). Molecular architecture of the rotary motor in ATP synthase. Science, 286, 1700-1705. PubMed id: 10576729 DOI: 10.1126/science.286.5445.1700
Date:
18-Aug-10     Release date:   22-Sep-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P07251  (ATPA_YEAST) -  ATP synthase subunit alpha, mitochondrial
Seq:
Struc:
 
Seq:
Struc:
545 a.a.
483 a.a.
Protein chains
Pfam   ArchSchema ?
P00830  (ATPB_YEAST) -  ATP synthase subunit beta, mitochondrial
Seq:
Struc:
511 a.a.
471 a.a.
Protein chain
Pfam   ArchSchema ?
P38077  (ATPG_YEAST) -  ATP synthase subunit gamma, mitochondrial
Seq:
Struc:
311 a.a.
266 a.a.
Protein chain
Pfam   ArchSchema ?
Q12165  (ATPD_YEAST) -  ATP synthase subunit delta, mitochondrial
Seq:
Struc:
160 a.a.
119 a.a.
Protein chain
Pfam   ArchSchema ?
E9P9X4  (E9P9X4_YEASX) -  ATP synthase catalytic sector F1 epsilon subunit
Seq:
Struc:
62 a.a.
49 a.a.
Protein chains
Pfam   ArchSchema ?
P61829  (ATP9_YEAST) -  ATP synthase subunit 9, mitochondrial
Seq:
Struc:
76 a.a.
73 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains D, E, F: E.C.3.6.3.14  - H(+)-transporting two-sector ATPase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O + H+(In) = ADP + phosphate + H+(Out)
ATP
Bound ligand (Het Group name = ANP)
matches with 93.00% similarity
+ H(2)O
+ H(+)(In)
= ADP
+ phosphate
+ H(+)(Out)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   16 terms 
  Biological process     transport   7 terms 
  Biochemical function     nucleotide binding     10 terms  

 

 
    reference    
 
 
DOI no: 10.1126/science.286.5445.1700 Science 286:1700-1705 (1999)
PubMed id: 10576729  
 
 
Molecular architecture of the rotary motor in ATP synthase.
D.Stock, A.G.Leslie, J.E.Walker.
 
  ABSTRACT  
 
Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F1 domain. An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits. Each c subunit forms an alpha-helical hairpin. The interhelical loops of six to seven of the c subunits are in close contact with the gamma and delta subunits of the central stalk. The extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis.
 
  Selected figure(s)  
 
Figure 2.
Fig. 2. Stereo views of an electron density map of the yeast F[1]c[10] complex. The solvent flattened map was calculated at 3.9 Å resolution and contoured at 1.5 . (A) Side view containing the bovine F[1] C model (with in orange, in yellow, and in green). The density of symmetry-related molecules in the crystal is masked out. The inset indicates the location of the subunits within the complex. The location of the section shown in (C) is indicated by the white box; the direction of the view is indicated by the arrow. The presumed membrane region (M) (2) is marked by the two dotted lines. The c subunits are numbered 3, 2, 1, 10, and 9 (the best ordered c subunit was chosen as number 1). The overall height of the complex is ~190 Å, of which the [3] [3] subcomplex accounts for 83 Å, the stalk for 50 Å, and the c subunits for 58 Å. (B) Enlarged view of the / -c contact region with the model (and numbering) of the E. coli subunit (in red) and the E. coli c subunit (in white) fitted into the density, contoured at 1.0 . The white box in the inset indicates the location of the displayed section within the complex. (C) End-on view of the density of the c ring. The inset shows the location of the , , , and subunits in relation to the c subunits. The helices of the c subunit are drawn as blue circles, the larger outer circles accounting for the larger side chains in the COOH-terminal helix. The outer diameter of the c ring is 55 Å (top) to 42 Å (equator) to 45 Å (bottom), and the inner diameter is 27 Å (top) to 17 Å (equator) to 22 Å (bottom). The dimensions exclude consideration of unresolved regions of density, including amino acid side chains and detergent or lipid molecules. The two regions of density near subunit 10 are not extensive and are likely to be noise.
Figure 3.
Fig. 3. Stereo view of the crystal packing of the yeast F[1]c[10] complex. A 45 Å thick section through the crystal perpendicular to the crystallographic y axis is shown. The electron density is contoured at 1.2 . The red lines mark the x and z axes of the crystal lattice. All figures were prepared with the program MAIN (72).
 
  The above figures are reprinted by permission from the AAAs: Science (1999, 286, 1700-1705) copyright 1999.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
23334411 S.Arai, S.Saijo, K.Suzuki, K.Mizutani, Y.Kakinuma, Y.Ishizuka-Katsura, N.Ohsawa, T.Terada, M.Shirouzu, S.Yokoyama, S.Iwata, I.Yamato, and T.Murata (2013).
Rotation mechanism of Enterococcus hirae V1-ATPase based on asymmetric crystal structures.
  Nature, 493, 703-707.
PDB codes: 3vr2 3vr3 3vr4 3vr5 3vr6
22504883 J.Symersky, V.Pagadala, D.Osowski, A.Krah, T.Meier, J.D.Faraldo-Gómez, and D.M.Mueller (2012).
Structure of the c(10) ring of the yeast mitochondrial ATP synthase in the open conformation.
  Nat Struct Mol Biol, 19, 485.
PDB codes: 3u2f 3u2y 3u32 3ud0
22850819 R.Rizzuto, D.De Stefani, A.Raffaello, and C.Mammucari (2012).
Mitochondria as sensors and regulators of calcium signalling.
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22178924 W.C.Lau, and J.L.Rubinstein (2012).
Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase.
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PDB code: 3j0j
21280123 C.S.Gandhi, T.A.Walton, and D.C.Rees (2011).
OCAM: A new tool for studying the oligomeric diversity of MscL channels.
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21502534 J.Czub, and H.Grubmüller (2011).
Torsional elasticity and energetics of F1-ATPase.
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21073359 M.Börsch (2011).
Single-molecule fluorescence resonance energy transfer techniques on rotary ATP synthases.
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21296189 M.Hüttemann, P.Pecina, M.Rainbolt, T.H.Sanderson, V.E.Kagan, L.Samavati, J.W.Doan, and I.Lee (2011).
The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: From respiration to apoptosis.
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21287678 R.Bienert, B.Zimmermann, V.Rombach-Riegraf, and P.Gräber (2011).
Time-Dependent FRET with Single Enzymes: Domain Motions and Catalysis in H(+) -ATP Synthases.
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21278755 T.Ibuki, K.Imada, T.Minamino, T.Kato, T.Miyata, and K.Namba (2011).
Common architecture of the flagellar type III protein export apparatus and F- and V-type ATPases.
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PDB code: 3ajw
20141757 B.A.Feniouk, Y.Kato-Yamada, M.Yoshida, and T.Suzuki (2010).
Conformational transitions of subunit epsilon in ATP synthase from thermophilic Bacillus PS3.
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20972431 D.Pogoryelov, A.Krah, J.D.Langer, ..Yildiz, J.D.Faraldo-Gómez, and T.Meier (2010).
Microscopic rotary mechanism of ion translocation in the F(o) complex of ATP synthases.
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PDB codes: 2xqs 2xqt 2xqu
20655344 D.W.Urry, K.D.Urry, W.Szaflarski, and M.Nowicki (2010).
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Physiological impact of intrinsic ADP inhibition of cyanobacterial FoF1 conferred by the inherent sequence inserted into the gammasubunit.
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20847295 I.N.Watt, M.G.Montgomery, M.J.Runswick, A.G.Leslie, and J.E.Walker (2010).
Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria.
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PDB code: 2xnd
20977480 J.S.Amthor (2010).
From sunlight to phytomass: on the potential efficiency of converting solar radiation to phyto-energy.
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19826804 K.McLuskey, A.W.Roszak, Y.Zhu, and N.W.Isaacs (2010).
Crystal structures of all-alpha type membrane proteins.
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20667175 K.R.Vinothkumar, and R.Henderson (2010).
Structures of membrane proteins.
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19875463 M.D'Aurelio, C.Vives-Bauza, M.M.Davidson, and G.Manfredi (2010).
Mitochondrial DNA background modifies the bioenergetics of NARP/MILS ATP6 mutant cells.
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21170312 M.D.Egbert, X.E.Barandiaran, and E.A.Di Paolo (2010).
A minimal model of metabolism-based chemotaxis.
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20118642 M.Maeda (2010).
H(+)-transporting ATP Synthases: Insights into How Their Electrochemically Driven Motor Might Serve as a Drug Target.
  Yakugaku Zasshi, 130, 191-197.  
20644710 P.Balabaskaran Nina, N.V.Dudkina, L.A.Kane, J.E.van Eyk, E.J.Boekema, M.W.Mather, and A.B.Vaidya (2010).
Highly divergent mitochondrial ATP synthase complexes in Tetrahymena thermophila.
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20533897 P.R.Rich, and A.Maréchal (2010).
The mitochondrial respiratory chain.
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21037553 R.Ishmukhametov, T.Hornung, D.Spetzler, and W.D.Frasch (2010).
Direct observation of stepped proteolipid ring rotation in E. coli F₀F₁-ATP synthase.
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20858734 S.J.Ferguson (2010).
ATP synthase: from sequence to ring size to the P/O ratio.
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20490637 S.Nath (2010).
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20080582 W.C.Lau, and J.L.Rubinstein (2010).
Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V(O) motor.
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20820716 Y.G.Shu, J.C.Yue, and Z.C.Ou-Yang (2010).
FoF1-ATPase, rotary motor and biosensor.
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20689227 Y.Kagawa (2010).
ATP synthase: from single molecule to human bioenergetics.
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21040305 Y.Pang, H.Wang, W.Q.Song, and Y.X.Zhu (2010).
The cotton ATP synthase δ1 subunit is required to maintain a higher ATP/ADP ratio that facilitates rapid fibre cell elongation.
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20596883 Y.Todokoro, M.Kobayashi, T.Sato, T.Kawakami, I.Yumen, S.Aimoto, T.Fujiwara, and H.Akutsu (2010).
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20705594 Z.Ma, M.Cao, Y.Liu, Y.He, Y.Wang, C.Yang, W.Wang, Y.Du, M.Zhou, and F.Gao (2010).
Mitochondrial F1Fo-ATP synthase translocates to cell surface in hepatocytes and has high activity in tumor-like acidic and hypoxic environment.
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19489730 C.von Ballmoos, A.Wiedenmann, and P.Dimroth (2009).
Essentials for ATP synthesis by F1F0 ATP synthases.
  Annu Rev Biochem, 78, 649-672.  
19995987 D.M.Rees, A.G.Leslie, and J.E.Walker (2009).
The structure of the membrane extrinsic region of bovine ATP synthase.
  Proc Natl Acad Sci U S A, 106, 21597-21601.
PDB code: 2wss
19783985 D.Pogoryelov, O.Yildiz, J.D.Faraldo-Gómez, and T.Meier (2009).
High-resolution structure of the rotor ring of a proton-dependent ATP synthase.
  Nat Struct Mol Biol, 16, 1068-1073.
PDB code: 2wie
19878046 D.Sengupta, A.Rampioni, and S.J.Marrink (2009).
Simulations of the c-subunit of ATP-synthase reveal helix rearrangements.
  Mol Membr Biol, 26, 422-434.  
19578988 F.Di Rocco, A.D.Zambelli, and L.B.Vidal Rioja (2009).
Identification of camelid specific residues in mitochondrial ATP synthase subunits.
  J Bioenerg Biomembr, 41, 223-228.  
19821035 J.C.Talbot, A.Dautant, A.Polidori, B.Pucci, T.Cohen-Bouhacina, A.Maali, B.Salin, D.Brèthes, J.Velours, and M.F.Giraud (2009).
Hydrogenated and fluorinated surfactants derived from Tris(hydroxymethyl)-acrylamidomethane allow the purification of a highly active yeast F1-F0 ATP-synthase with an enhanced stability.
  J Bioenerg Biomembr, 41, 349-360.  
19348765 J.G.Wise, and P.D.Vogel (2009).
Accommodating discontinuities in dimeric left-handed coiled coils in ATP synthase external stalks.
  Biophys J, 96, 2823-2831.  
19176524 J.Liu, M.Fujisawa, D.B.Hicks, and T.A.Krulwich (2009).
Characterization of the Functionally Critical AXAXAXA and PXXEXXP Motifs of the ATP Synthase c-Subunit from an Alkaliphilic Bacillus.
  J Biol Chem, 284, 8714-8725.  
19203996 J.Vonck, K.Y.Pisa, N.Morgner, B.Brutschy, and V.Müller (2009).
Three-dimensional structure of A1A0 ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy.
  J Biol Chem, 284, 10110-10119.  
19362069 L.Bae, and S.B.Vik (2009).
A more robust version of the Arginine 210-switched mutant in subunit a of the Escherichia coli ATP synthase.
  Biochim Biophys Acta, 1787, 1129-1134.  
20040113 M.Freigassner, H.Pichler, and A.Glieder (2009).
wTuning microbial hosts for membrane protein production.
  Microb Cell Fact, 8, 69.  
20166550 M.Murata, Y.Miwa, and I.Sato (2009).
Expression of respiratory chain enzyme mRNA and the morphological properties of mitochondria in the masseter muscles of klotho mutant mice.
  Okajimas Folia Anat Jpn, 86, 93.  
18672007 M.Rak, X.Zeng, J.J.Brière, and A.Tzagoloff (2009).
Assembly of F0 in Saccharomyces cerevisiae.
  Biochim Biophys Acta, 1793, 108-116.  
19423706 M.Vollmar, D.Schlieper, M.Winn, C.Büchner, and G.Groth (2009).
Structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase.
  J Biol Chem, 284, 18228-18235.
PDB code: 2w5j
19128495 N.R.Boyle, and J.A.Morgan (2009).
Flux balance analysis of primary metabolism in Chlamydomonas reinhardtii.
  BMC Syst Biol, 3, 4.  
19542218 P.R.Steed, and R.H.Fillingame (2009).
Aqueous accessibility to the transmembrane regions of subunit c of the Escherichia coli F1F0 ATP synthase.
  J Biol Chem, 284, 23243-23250.  
19458709 S.H.White (2009).
Biophysical dissection of membrane proteins.
  Nature, 459, 344-346.  
19233840 V.Kabaleeswaran, H.Shen, J.Symersky, J.E.Walker, A.G.Leslie, and D.M.Mueller (2009).
Asymmetric structure of the yeast F1 ATPase in the absence of bound nucleotides.
  J Biol Chem, 284, 10546-10551.
PDB code: 3fks
19701184 Z.Liu, C.S.Gandhi, and D.C.Rees (2009).
Structure of a tetrameric MscL in an expanded intermediate state.
  Nature, 461, 120-124.
PDB code: 3hzq
18380897 A.Y.Mulkidjanian, M.Y.Galperin, K.S.Makarova, Y.I.Wolf, and E.V.Koonin (2008).
Evolutionary primacy of sodium bioenergetics.
  Biol Direct, 3, 13.  
18485887 A.Y.Mulkidjanian, P.Dibrov, and M.Y.Galperin (2008).
The past and present of sodium energetics: may the sodium-motive force be with you.
  Biochim Biophys Acta, 1777, 985-992.  
18431494 B.J.van Raam, W.Sluiter, E.de Wit, D.Roos, A.J.Verhoeven, and T.W.Kuijpers (2008).
Mitochondrial membrane potential in human neutrophils is maintained by complex III activity in the absence of supercomplex organisation.
  PLoS ONE, 3, e2013.  
18573072 C.von Ballmoos, G.M.Cook, and P.Dimroth (2008).
Unique rotary ATP synthase and its biological diversity.
  Annu Rev Biophys, 37, 43-64.  
18721138 D.Pogoryelov, Y.Nikolaev, U.Schlattner, K.Pervushin, P.Dimroth, and T.Meier (2008).
Probing the rotor subunit interface of the ATP synthase from Ilyobacter tartaricus.
  FEBS J, 275, 4850-4862.  
19001275 H.Sielaff, H.Rennekamp, A.Wächter, H.Xie, F.Hilbers, K.Feldbauer, S.D.Dunn, S.Engelbrecht, and W.Junge (2008).
Domain compliance and elastic power transmission in rotary F(O)F(1)-ATPase.
  Proc Natl Acad Sci U S A, 105, 17760-17765.  
18723591 H.Sielaff, H.Rennekamp, S.Engelbrecht, and W.Junge (2008).
Functional halt positions of rotary FOF1-ATPase correlated with crystal structures.
  Biophys J, 95, 4979-4987.  
18628203 J.A.Scanlon, M.K.Al-Shawi, and R.K.Nakamoto (2008).
A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysis.
  J Biol Chem, 283, 26228-26240.  
  19669503 J.J.García-Trejo, and E.Morales-Ríos (2008).
Regulation of the F(1)F (0)-ATP Synthase Rotary Nanomotor in its Monomeric-Bacterial and Dimeric-Mitochondrial Forms.
  J Biol Phys, 34, 197-212.  
18768789 J.K.Lee, G.I.Belogrudov, and R.M.Stroud (2008).
Crystal structure of bovine mitochondrial factor B at 0.96-A resolution.
  Proc Natl Acad Sci U S A, 105, 13379-13384.
PDB codes: 3dze 3e2j 3e3z 3e4g
18156183 K.C.Jefferies, and M.Forgac (2008).
Subunit H of the vacuolar (H+) ATPase inhibits ATP hydrolysis by the free V1 domain by interaction with the rotary subunit F.
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18355313 M.Fritz, A.L.Klyszejko, N.Morgner, J.Vonck, B.Brutschy, D.J.Muller, T.Meier, and V.Müller (2008).
An intermediate step in the evolution of ATPases: a hybrid F(0)-V(0) rotor in a bacterial Na(+) F(1)F(0) ATP synthase.
  FEBS J, 275, 1999-2007.  
18431549 M.Maeda (2008).
ATP synthases: bioinformatic based insights into how their electrochemically driven motor comprised of subunits a and c might serve as a drug target.
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18339602 M.Nakanishi-Matsui, and M.Futai (2008).
Stochastic rotational catalysis of proton pumping F-ATPase.
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18323778 M.Strauss, G.Hofhaus, R.R.Schröder, and W.Kühlbrandt (2008).
Dimer ribbons of ATP synthase shape the inner mitochondrial membrane.
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18235435 N.E.Chayen, and E.Saridakis (2008).
Protein crystallization: from purified protein to diffraction-quality crystal.
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18178144 O.Y.Dmitriev, K.H.Freedman, J.Hermolin, and R.H.Fillingame (2008).
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18332132 P.R.Steed, and R.H.Fillingame (2008).
Subunit a facilitates aqueous access to a membrane-embedded region of subunit c in Escherichia coli F1F0 ATP synthase.
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18515057 R.K.Nakamoto, J.A.Baylis Scanlon, and M.K.Al-Shawi (2008).
The rotary mechanism of the ATP synthase.
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18068111 R.R.Ishmukhametov, J.B.Pond, A.Al-Huqail, M.A.Galkin, and S.B.Vik (2008).
ATP synthesis without R210 of subunit a in the Escherichia coli ATP synthase.
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The new unified theory of ATP synthesis/hydrolysis and muscle contraction, its manifold fundamental consequences and mechanistic implications and its applications in health and disease.
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18316723 S.Steigmiller, P.Turina, and P.Gräber (2008).
The thermodynamic H+/ATP ratios of the H+-ATPsynthases from chloroplasts and Escherichia coli.
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18326647 T.Hornung, O.A.Volkov, T.M.Zaida, S.Delannoy, J.G.Wise, and P.D.Vogel (2008).
Structure of the cytosolic part of the subunit b-dimer of Escherichia coli F0F1-ATP synthase.
  Biophys J, 94, 5053-5064.  
18471428 T.Hornung, R.Ishmukhametov, D.Spetzler, J.Martin, and W.D.Frasch (2008).
Determination of torque generation from the power stroke of Escherichia coli F1-ATPase.
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19325821 T.Mitsui, and H.Ohshima (2008).
Shear stress transmission model for the flagellar rotary motor.
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18085722 V.Balzani, A.Credi, and M.Venturi (2008).
Molecular machines working on surfaces and at interfaces.
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Photochemical conversion of solar energy.
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Yeast cells depleted in Atp14p fail to assemble Atp6p within the ATP synthase and exhibit altered mitochondrial cristae morphology.
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17697996 A.Stocker, S.Keis, J.Vonck, G.M.Cook, and P.Dimroth (2007).
The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase.
  Structure, 15, 904-914.
PDB code: 2qe7
17545285 D.Pogoryelov, C.Reichen, A.L.Klyszejko, R.Brunisholz, D.J.Muller, P.Dimroth, and T.Meier (2007).
The oligomeric state of c rings from cyanobacterial F-ATP synthases varies from 13 to 15.
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17411433 J.B.Pereira-Leal, E.D.Levy, C.Kamp, and S.A.Teichmann (2007).
Evolution of protein complexes by duplication of homomeric interactions.
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12220197 Y.Arata, J.D.Baleja, and M.Forgac (2002).
Localization of subunits D, E, and G in the yeast V-ATPase complex using cysteine-mediated cross-linking to subunit B.
  Biochemistry, 41, 11301-11307.  
12231509 Y.Chaban, T.Ubbink-Kok, W.Keegstra, J.S.Lolkema, and E.J.Boekema (2002).
Composition of the central stalk of the Na+-pumping V-ATPase from Caloramator fervidus.
  EMBO Rep, 3, 982-987.  
11785753 A.Arora, and L.K.Tamm (2001).
Biophysical approaches to membrane protein structure determination.
  Curr Opin Struct Biol, 11, 540-547.  
11580837 A.J.Martín-Galiano, M.J.Ferrándiz, and A.G.de la Campa (2001).
The promoter of the operon encoding the F0F1 ATPase of Streptococcus pneumoniae is inducible by pH.
  Mol Microbiol, 41, 1327-1338.  
11331012 A.M.Grosset, B.R.Gibney, F.Rabanal, C.C.Moser, and P.L.Dutton (2001).
Proof of principle in a de novo designed protein maquette: an allosterically regulated, charge-activated conformational switch in a tetra-alpha-helix bundle.
  Biochemistry, 40, 5474-5487.  
11320317 A.Rodgers, G.Ewart, G.Cox, and M.Wilce (2001).
Crystallization and preliminary X-ray analysis of the complex of the epsilon-subunit and the central domain of the gamma-subunit from the Escherichia coli ATP synthase.
  Acta Crystallogr D Biol Crystallogr, 57, 722-724.  
11340051 B.E.Schultz, and S.I.Chan (2001).
Structures and proton-pumping strategies of mitochondrial respiratory enzymes.
  Annu Rev Biophys Biomol Struct, 30, 23-65.  
11828469 B.Ludwig, E.Bender, S.Arnold, M.Hüttemann, I.Lee, and B.Kadenbach (2001).
Cytochrome C oxidase and the regulation of oxidative phosphorylation.
  Chembiochem, 2, 392-403.  
  11415978 C.G.Tate (2001).
A feast of membrane protein structures in Madrid. Workshop: Pumps, channels and transporters: structure and function.
  EMBO Rep, 2, 476-480.  
11509340 D.A.Cherepanov, and W.Junge (2001).
Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: curvature as an indicator of the torque.
  Biophys J, 81, 1234-1244.  
11735378 E.A.Schon, S.Santra, F.Pallotti, and M.E.Girvin (2001).
Pathogenesis of primary defects in mitochondrial ATP synthesis.
  Semin Cell Dev Biol, 12, 441-448.  
11742976 E.Cabezón, M.J.Runswick, A.G.Leslie, and J.E.Walker (2001).
The structure of bovine IF(1), the regulatory subunit of mitochondrial F-ATPase.
  EMBO J, 20, 6990-6996.
PDB code: 1gmj
11695186 F.Schuler, and J.E.Casida (2001).
The insecticide target in the PSST subunit of complex I.
  Pest Manag Sci, 57, 932-940.  
11248192 G.Kaim (2001).
The Na(+)-translocating F(1)F(0) ATP synthase of Propionigenium modestum: mechanochemical insights into the F(0) motor that drives ATP synthesis.
  Biochim Biophys Acta, 1505, 94.  
11266365 H.Stahlberg, D.J.Müller, K.Suda, D.Fotiadis, A.Engel, T.Meier, U.Matthey, and P.Dimroth (2001).
Bacterial Na(+)-ATP synthase has an undecameric rotor.
  EMBO Rep, 2, 229-233.  
11377800 I.E.Scheffler (2001).
Mitochondria make a come back.
  Adv Drug Deliv Rev, 49, 3.  
11438702 M.L.Hutcheon, T.M.Duncan, H.Ngai, and R.L.Cross (2001).
Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the F(O) sector of Escherichia coli ATP synthase.
  Proc Natl Acad Sci U S A, 98, 8519-8524.  
11337406 M.Maeshima (2001).
TONOPLAST TRANSPORTERS: Organization and Function.
  Annu Rev Plant Physiol Plant Mol Biol, 52, 469-497.  
11245786 N.Arakaki, Y.Ueyama, M.Hirose, T.Himeda, H.Shibata, S.Futaki, K.Kitagawa, and T.Higuti (2001).
Stoichiometry of subunit e in rat liver mitochondrial H(+)-ATP synthase and membrane topology of its putative Ca(2+)-dependent regulatory region.
  Biochim Biophys Acta, 1504, 220-228.  
11509339 O.Pänke, D.A.Cherepanov, K.Gumbiowski, S.Engelbrecht, and W.Junge (2001).
Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: angular torque profile of the enzyme.
  Biophys J, 81, 1220-1233.  
11160082 P.C.Jones (2001).
Introduction of a carboxyl group in the first transmembrane helix of Escherichia coli F1Fo ATPase subunit c and cytoplasmic pH regulation.
  J Bacteriol, 183, 1524-1530.  
11545726 P.D.Boyer (2001).
New insights into one of nature's remarkable catalysts, the ATP synthase.
  Mol Cell, 8, 246-247.  
11509182 R.I.Menz, J.E.Walker, and A.G.Leslie (2001).
Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis.
  Cell, 106, 331-341.
PDB code: 1h8e
11746826 R.J.Bienstock, and J.C.Barrett (2001).
KAI1, a prostate metastasis suppressor: prediction of solvated structure and interactions with binding partners; integrins, cadherins, and cell-surface receptor proteins.
  Mol Carcinog, 32, 139-153.  
11141070 S.D.Dunn, E.Kellner, and H.Lill (2001).
Specific heterodimer formation by the cytoplasmic domains of the b and b' subunits of cyanobacterial ATP synthase.
  Biochemistry, 40, 187-192.  
11592980 S.Kawasaki-Nishi, T.Nishi, and M.Forgac (2001).
Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation.
  Proc Natl Acad Sci U S A, 98, 12397-12402.  
11381110 S.P.Tsunoda, A.J.Rodgers, R.Aggeler, M.C.Wilce, M.Yoshida, and R.A.Capaldi (2001).
Large conformational changes of the epsilon subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme.
  Proc Natl Acad Sci U S A, 98, 6560-6564.  
11158567 S.P.Tsunoda, R.Aggeler, M.Yoshida, and R.A.Capaldi (2001).
Rotation of the c subunit oligomer in fully functional F1Fo ATP synthase.
  Proc Natl Acad Sci U S A, 98, 898-902.  
11274449 T.D.Bunney, H.S.van Walraven, and A.H.de Boer (2001).
14-3-3 protein is a regulator of the mitochondrial and chloroplast ATP synthase.
  Proc Natl Acad Sci U S A, 98, 4249-4254.  
11933249 V.Balzani, and A.Credi (2001).
Artificial molecular-level machines.
  Chem Rec, 1, 422-435.  
11248193 V.Müller, S.Aufurth, and S.Rahlfs (2001).
The Na(+) cycle in Acetobacterium woodii: identification and characterization of a Na(+) translocating F(1)F(0)-ATPase with a mixed oligomer of 8 and 16 kDa proteolipids.
  Biochim Biophys Acta, 1505, 108-120.  
11320246 W.Jiang, J.Hermolin, and R.H.Fillingame (2001).
The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10.
  Proc Natl Acad Sci U S A, 98, 4966-4971.  
11029588 A.N.Stephens, X.Roucou, I.M.Artika, R.J.Devenish, and P.Nagley (2000).
Topology and proximity relationships of yeast mitochondrial ATP synthase subunit 8 determined by unique introduced cysteine residues.
  Eur J Biochem, 267, 6443-6451.  
10825454 A.Poetsch, D.Neff, H.Seelert, H.Schägger, and N.A.Dencher (2000).
Dye removal, catalytic activity and 2D crystallization of chloroplast H(+)-ATP synthase purified by blue native electrophoresis.
  Biochim Biophys Acta, 1466, 339-349.  
10981630 C.R.Lowe (2000).
Nanobiotechnology: the fabrication and applications of chemical and biological nanostructures.
  Curr Opin Struct Biol, 10, 428-434.  
11114504 D.Stock, C.Gibbons, I.Arechaga, A.G.Leslie, and J.E.Walker (2000).
The rotary mechanism of ATP synthase.
  Curr Opin Struct Biol, 10, 672-679.  
11084368 E.A.Schon (2000).
Mitochondrial genetics and disease.
  Trends Biochem Sci, 25, 555-560.  
10984595 E.Pebay-Peyroula, R.Neutze, and E.M.Landau (2000).
Lipidic cubic phase crystallization of bacteriorhodopsin and cryotrapping of intermediates: towards resolving a revolving photocycle.
  Biochim Biophys Acta, 1460, 119-132.  
10913268 G.Grüber, M.Radermacher, T.Ruiz, J.Godovac-Zimmermann, B.Canas, D.Kleine-Kohlbrecher, M.Huss, W.R.Harvey, and H.Wieczorek (2000).
Three-dimensional structure and subunit topology of the V(1) ATPase from Manduca sexta midgut.
  Biochemistry, 39, 8609-8616.  
10836505 G.Oster, H.Wang, and M.Grabe (2000).
How Fo-ATPase generates rotary torque.
  Philos Trans R Soc Lond B Biol Sci, 355, 523-528.  
10984599 H.Kandori (2000).
Role of internal water molecules in bacteriorhodopsin.
  Biochim Biophys Acta, 1460, 177-191.  
10806404 J.C.Greie, G.Deckers-Hebestreit, and K.Altendorf (2000).
Secondary structure composition of reconstituted subunit b of the Escherichia coli ATP synthase.
  Eur J Biochem, 267, 3040-3048.  
10966478 J.L.Popot, and D.M.Engelman (2000).
Helical membrane protein folding, stability, and evolution.
  Annu Rev Biochem, 69, 881-922.  
10759867 J.Lai-Zhang, and D.M.Mueller (2000).
Complementation of deletion mutants in the genes encoding the F1-ATPase by expression of the corresponding bovine subunits in yeast S. cerevisiae.
  Eur J Biochem, 267, 2409-2418.  
10819998 J.Weber, and A.E.Senior (2000).
Features of F(1)-ATPase catalytic and noncatalytic sites revealed by fluorescence lifetimes and acrylamide quenching of specifically inserted tryptophan residues.
  Biochemistry, 39, 5287-5294.  
10836501 K.Kinosita, R.Yasuda, H.Noji, and K.Adachi (2000).
A rotary molecular motor that can work at near 100% efficiency.
  Philos Trans R Soc Lond B Biol Sci, 355, 473-489.  
10757988 K.M.Cunningham, and R.E.McCarty (2000).
Influences of energization and nucleotide binding on the reaction of Lucifer Yellow vinyl sulfone with the alpha subunits of the chloroplast ATP synthase.
  Biochemistry, 39, 4391-4398.  
10852722 L.A.Sazanov, S.Y.Peak-Chew, I.M.Fearnley, and J.E.Walker (2000).
Resolution of the membrane domain of bovine complex I into subcomplexes: implications for the structural organization of the enzyme.
  Biochemistry, 39, 7229-7235.  
10827963 M.Grabe, H.Wang, and G.Oster (2000).
The mechanochemistry of V-ATPase proton pumps.
  Biophys J, 78, 2798-2813.  
10997900 P.A.Buckley, J.Baz Jackson, T.Schneider, S.A.White, D.W.Rice, and P.J.Baker (2000).
Protein-protein recognition, hydride transfer and proton pumping in the transhydrogenase complex.
  Structure, 8, 809-815.
PDB code: 1f8g
11004469 P.Dimroth, U.Matthey, and G.Kaim (2000).
Critical evaluation of the one- versus the two-channel model for the operation of the ATP synthase's F(o) motor.
  Biochim Biophys Acta, 1459, 506-513.  
10747812 P.Paumard, J.Vaillier, C.Napias, G.Arselin, D.Brèthes, P.V.Graves, and J.Velours (2000).
Environmental study of subunit i, a F(o) component of the yeast ATP synthase.
  Biochemistry, 39, 4199-4205.  
10782087 R.A.Capaldi (2000).
The changing face of mitochondrial research.
  Trends Biochem Sci, 25, 212-214.  
11004471 S.D.Dunn, Y.Bi, and M.Revington (2000).
A re-examination of the structural and functional consequences of mutation of alanine-128 of the b subunit of Escherichia coli ATP synthase to aspartic acid.
  Biochim Biophys Acta, 1459, 521-527.  
11084356 S.J.Ferguson (2000).
ATP synthase: what dictates the size of a ring?
  Curr Biol, 10, R804-R808.  
11082207 T.Himeda, K.Morokami, N.Arakaki, H.Shibata, and T.Higuti (2000).
Synchronized transcriptional gene expression of H+-ATP synthase subunits in different tissues of Fischer 344 rats of different ages.
  Eur J Biochem, 267, 6938-6942.  
10981634 T.M.Iverson, C.Luna-Chavez, I.Schröder, G.Cecchini, and D.C.Rees (2000).
Analyzing your complexes: structure of the quinol-fumarate reductase respiratory complex.
  Curr Opin Struct Biol, 10, 448-455.  
10673443 T.Ohnishi, C.C.Moser, C.C.Page, P.L.Dutton, and T.Yano (2000).
Simple redox-linked proton-transfer design: new insights from structures of quinol-fumarate reductase.
  Structure, 8, R23-R32.  
10880968 T.Xu, F.Zanotti, A.Gaballo, G.Raho, and S.Papa (2000).
F1 and F0 connections in the bovine mitochondrial ATP synthase: the role of the of alpha subunit N-terminus, oligomycin-sensitivity conferring protein (OCSP) and subunit d.
  Eur J Biochem, 267, 4445-4455.  
11091368 V.Balzani, A.Credi, F.M.Raymo, and J.F.Stoddart (2000).
Artificial Molecular Machines.
  Angew Chem Int Ed Engl, 39, 3348-3391.  
10995251 Y.B.Peskova, and R.K.Nakamoto (2000).
Catalytic control and coupling efficiency of the Escherichia coli FoF1 ATP synthase: influence of the Fo sector and epsilon subunit on the catalytic transition state.
  Biochemistry, 39, 11830-11836.  
10747017 Z.G.Wang, D.Sheluho, D.L.Gatti, and S.H.Ackerman (2000).
The alpha-subunit of the mitochondrial F(1) ATPase interacts directly with the assembly factor Atp12p.
  EMBO J, 19, 1486-1493.  
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