PDBsum entry 1c17

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protein Protein-protein interface(s) links
Membrane protein PDB id
Protein chains
(+ 6 more) 79 a.a. *
142 a.a. *
* Residue conservation analysis
PDB id:
Name: Membrane protein
Title: A1c12 subcomplex of f1fo atp synthase
Structure: Atp synthase subunit c. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Engineered: yes. Atp synthase subunit a. Chain: m. Fragment: consensus helices of subunit a. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
NMR struc: 1 models
Authors: V.K.Rastogi,M.E.Girvin
Key ref:
V.K.Rastogi and M.E.Girvin (1999). Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature, 402, 263-268. PubMed id: 10580496 DOI: 10.1038/46224
20-Jul-99     Release date:   24-Nov-99    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P68699  (ATPL_ECOLI) -  ATP synthase subunit c
79 a.a.
79 a.a.
Protein chain
Pfam   ArchSchema ?
P0AB98  (ATP6_ECOLI) -  ATP synthase subunit a
271 a.a.
142 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   5 terms 
  Biological process     transport   6 terms 
  Biochemical function     lipid binding     4 terms  


DOI no: 10.1038/46224 Nature 402:263-268 (1999)
PubMed id: 10580496  
Structural changes linked to proton translocation by subunit c of the ATP synthase.
V.K.Rastogi, M.E.Girvin.
F1F0 ATP synthases use a transmembrane proton gradient to drive the synthesis of cellular ATP. The structure of the cytosolic F1 portion of the enzyme and the basic mechanism of ATP hydrolysis by F1 are now well established, but how proton translocation through the transmembrane F0 portion drives these catalytic changes is less clear. Here we describe the structural changes in the proton-translocating F0 subunit c that are induced by deprotonating the specific aspartic acid involved in proton transport. Conformational changes between the protonated and deprotonated forms of subunit c provide the structural basis for an explicit mechanism to explain coupling of proton translocation by F0 to the rotation of subunits within the core of F1. Rotation of these subunits within F1 causes the catalytic conformational changes in the active sites of F1 that result in ATP synthesis.
  Selected figure(s)  
Figure 1.
Figure 1 Schematic diagram of F[1]F[O] ATP synthase. Subunits shown in white are thought to remain fixed with respect to each other during proton translocation and ATP synthesis. Subunits shown in grey are thought to rotate as a unit with respect to the fixed subunits during catalysis.
Figure 4.
Figure 4 Models for the c[12] and ac[12] subcomplexes of F[O]. a, Model of the c[12] oligomer, with the Asp 61-deprotonated subunit coloured in red, facing the viewer. The Asp 61 side chains are also shown for several subunits. Residues that can form disulphide cross links to subunit a are indicated with yellow spheres in the deprotonated subunit c and green spheres in the protonated subunit c. b, Region surrounding the deprotonated Asp 61 in the c[12] complex. Ribbon traces show the backbone from residues 22-30 and 56-64. Note that the deprotonated Asp 61 side chain (on left) is rotated 140° clockwise from its position in the adjacent monomer viewed from the polar loop. c, Alpha carbon traces of the best nine structural models of subunit a. Only the transmembrane segments and the Arg 210 side chains are shown. d, Side view of the ac[12] complex. Subunit a is shown in green, the deprotonated subunit c in red and its protonated neighbour in purple. The residues that can form cysteine disulphide cross links are indicated as yellow spheres in subunit c and pink spheres in subunit a. e, Top view of ribbon diagram of the ac[12] complex, with same colouring scheme as in d. The figure was prepared using Molscript50.
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nature (1999, 402, 263-268) copyright 1999.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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
21389271 D.G.Isom, C.A.Castañeda, B.R.Cannon, and B.García-Moreno E (2011).
Large shifts in pKa values of lysine residues buried inside a protein.
  Proc Natl Acad Sci U S A, 108, 5260-5265.  
20178386 C.Huang, and S.Mohanty (2010).
Challenging the limit: NMR assignment of a 31 kDa helical membrane protein.
  J Am Chem Soc, 132, 3662-3663.  
20972431 D.Pogoryelov, A.Krah, J.D.Langer, Ã.–.Yildiz, J.D.Faraldo-Gómez, and T.Meier (2010).
Microscopic rotary mechanism of ion translocation in the F(o) complex of ATP synthases.
  Nat Chem Biol, 6, 891-899.
PDB codes: 2xqs 2xqt 2xqu
20173764 L.K.Lee, A.G.Stewart, M.Donohoe, R.A.Bernal, and D.Stock (2010).
The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase.
  Nat Struct Mol Biol, 17, 373-378.
PDB code: 3k5b
20545867 L.van Niftrik, M.van Helden, S.Kirchen, E.G.van Donselaar, H.R.Harhangi, R.I.Webb, J.A.Fuerst, H.J.Op den Camp, M.S.Jetten, and M.Strous (2010).
Intracellular localization of membrane-bound ATPases in the compartmentalized anammox bacterium 'Candidatus Kuenenia stuttgartiensis'.
  Mol Microbiol, 77, 701-715.  
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.
  Proc Natl Acad Sci U S A, 107, 1367-1372.  
20336770 Y.Ito, and M.Ikeguchi (2010).
Structural fluctuation and concerted motions in F(1)-ATPase: A molecular dynamics study.
  J Comput Chem, 31, 2175-2185.  
20514364 Y.Meng, and A.E.Roitberg (2010).
Constant pH replica exchange molecular dynamics in biomolecules using a discrete protonation model.
  J Chem Theory Comput, 6, 1401-1412.  
20596883 Y.Todokoro, M.Kobayashi, T.Sato, T.Kawakami, I.Yumen, S.Aimoto, T.Fujiwara, and H.Akutsu (2010).
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H(+)-ATP synthase by solid-state NMR.
  J Biomol NMR, 48, 1.  
19489730 C.von Ballmoos, A.Wiedenmann, and P.Dimroth (2009).
Essentials for ATP synthesis by F1F0 ATP synthases.
  Annu Rev Biochem, 78, 649-672.  
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.  
19403800 E.S.Unal, R.Zhao, and I.D.Goldman (2009).
Role of the glutamate 185 residue in proton translocation mediated by the proton-coupled folate transporter SLC46A1.
  Am J Physiol Cell Physiol, 297, C66-C74.  
  20161395 H.J.Kim, S.C.Howell, W.D.Van Horn, Y.H.Jeon, and C.R.Sanders (2009).
Recent Advances in the Application of Solution NMR Spectroscopy to Multi-Span Integral Membrane Proteins.
  Prog Nucl Magn Reson Spectrosc, 55, 335-360.  
19160410 M.E.Vazquez-Memije, T.Rizza, M.C.Meschini, C.Nesti, F.M.Santorelli, and R.Carrozzo (2009).
Cellular and functional analysis of four mutations located in the mitochondrial ATPase6 gene.
  J Cell Biochem, 106, 878-886.  
19177365 M.Sagermann, R.R.Chapleau, E.DeLorimier, and M.Lei (2009).
Using affinity chromatography to engineer and characterize pH-dependent protein switches.
  Protein Sci, 18, 217-228.
PDB codes: 3crt 3cru 3d0z
19626676 M.Sikorska, J.K.Sandhu, D.K.Simon, V.Pathiraja, C.Sodja, Y.Li, M.Ribecco-Lutkiewicz, P.Lanthier, H.Borowy-Borowski, A.Upton, S.Raha, S.M.Pulst, and M.A.Tarnopolsky (2009).
Identification of ataxia-associated mtDNA mutations (m.4052T>C and m.9035T>C) and evaluation of their pathogenicity in transmitochondrial cybrids.
  Muscle Nerve, 40, 381-394.  
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
18641078 A.Damjanović, X.Wu, B.García-Moreno E, and B.R.Brooks (2008).
Backbone relaxation coupled to the ionization of internal groups in proteins: a self-guided Langevin dynamics study.
  Biophys J, 95, 4091-4101.  
18770013 A.Muhlia-Almazan, O.Martinez-Cruz, M.d.e. .L.Navarrete Del Toro, F.Garcia-Carreño, R.Arreola, R.Sotelo-Mundo, and G.Yepiz-Plascencia (2008).
Nuclear and mitochondrial subunits from the white shrimp Litopenaeus vannamei F(0)F (1) ATP-synthase complex: cDNA sequence, molecular modeling, and mRNA quantification of atp9 and atp6.
  J Bioenerg Biomembr, 40, 359-369.  
18851079 A.Y.Smirnov, S.Savel'ev, L.G.Mourokh, and F.Nori (2008).
Proton transport and torque generation in rotary biomotors.
  Phys Rev E Stat Nonlin Soft Matter Phys, 78, 031921.  
18937032 C.Zou, F.Naider, and O.Zerbe (2008).
Biosynthesis and NMR-studies of a double transmembrane domain from the Y4 receptor, a human GPCR.
  J Biomol NMR, 42, 257-269.  
18843528 M.Hüttemann, I.Lee, A.Pecinova, P.Pecina, K.Przyklenk, and J.W.Doan (2008).
Regulation of oxidative phosphorylation, the mitochondrial membrane potential, and their role in human disease.
  J Bioenerg Biomembr, 40, 445-456.  
18310246 M.Kobayashi, A.V.Struts, T.Fujiwara, M.F.Brown, and H.Akutsu (2008).
Fluid mechanical matching of H+-ATP synthase subunit c-ring with lipid membranes revealed by 2H solid-state NMR.
  Biophys J, 94, 4339-4347.  
18178144 O.Y.Dmitriev, K.H.Freedman, J.Hermolin, and R.H.Fillingame (2008).
Interaction of transmembrane helices in ATP synthase subunit a in solution as revealed by spin label difference NMR.
  Biochim Biophys Acta, 1777, 227-237.  
18273680 Q.Zhang, H.S.Atreya, D.E.Kamen, M.E.Girvin, and T.Szyperski (2008).
GFT projection NMR based resonance assignment of membrane proteins: application to subunit C of E. coli F(1)F (0) ATP synthase in LPPG micelles.
  J Biomol NMR, 40, 157-163.  
18515057 R.K.Nakamoto, J.A.Baylis Scanlon, and M.K.Al-Shawi (2008).
The rotary mechanism of the ATP synthase.
  Arch Biochem Biophys, 476, 43-50.  
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.
  Biochim Biophys Acta, 1777, 32-38.  
18316723 S.Steigmiller, P.Turina, and P.Gräber (2008).
The thermodynamic H+/ATP ratios of the H+-ATPsynthases from chloroplasts and Escherichia coli.
  Proc Natl Acad Sci U S A, 105, 3745-3750.  
18384384 T.Vorburger, J.Z.Ebneter, A.Wiedenmann, D.Morger, G.Weber, K.Diederichs, P.Dimroth, and C.von Ballmoos (2008).
Arginine-induced conformational change in the c-ring/a-subunit interface of ATP synthase.
  FEBS J, 275, 2137-2150.  
18085722 V.Balzani, A.Credi, and M.Venturi (2008).
Molecular machines working on surfaces and at interfaces.
  Chemphyschem, 9, 202-220.  
18922471 Y.Zhou, T.Cierpicki, R.H.Jimenez, S.M.Lukasik, J.F.Ellena, D.S.Cafiso, H.Kadokura, J.Beckwith, and J.H.Bushweller (2008).
NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation.
  Mol Cell, 31, 896-908.
PDB codes: 2k73 2k74
  17316427 A.Olgun (2007).
Biological effects of deuteronation: ATP synthase as an example.
  Theor Biol Med Model, 4, 9.  
17172297 D.A.Karp, A.G.Gittis, M.R.Stahley, C.A.Fitch, W.E.Stites, and B.García-Moreno E (2007).
High apparent dielectric constant inside a protein reflects structural reorganization coupled to the ionization of an internal Asp.
  Biophys J, 92, 2041-2053.
PDB code: 2oxp
17208001 J.Weber (2007).
ATP synthase--the structure of the stator stalk.
  Trends Biochem Sci, 32, 53-56.  
18240421 M.Hüttemann, I.Lee, L.Samavati, H.Yu, and J.W.Doan (2007).
Regulation of mitochondrial oxidative phosphorylation through cell signaling.
  Biochim Biophys Acta, 1773, 1701-1720.  
17387738 Jonge, L.H.Koymans, J.E.Guillemont, A.Koul, and K.Andries (2007).
A computational model of the inhibition of Mycobacterium tuberculosis ATPase by a new drug candidate R207910.
  Proteins, 67, 971-980.  
17893141 O.D.Vincent, B.E.Schwem, P.R.Steed, W.Jiang, and R.H.Fillingame (2007).
Fluidity of structure and swiveling of helices in the subunit c ring of Escherichia coli ATP synthase as revealed by cysteine-cysteine cross-linking.
  J Biol Chem, 282, 33788-33794.  
17766379 O.Y.Dmitriev, and R.H.Fillingame (2007).
The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c.
  Protein Sci, 16, 2118-2122.  
17035244 B.E.Schwem, and R.H.Fillingame (2006).
Cross-linking between helices within subunit a of Escherichia coli ATP synthase defines the transmembrane packing of a four-helix bundle.
  J Biol Chem, 281, 37861-37867.  
16826539 C.R.Sanders, and F.Sönnichsen (2006).
Solution NMR of membrane proteins: practice and challenges.
  Magn Reson Chem, 44, S24-S40.  
16843896 D.K.Clare, E.V.Orlova, M.A.Finbow, M.A.Harrison, J.B.Findlay, and H.R.Saibil (2006).
An expanded and flexible form of the vacuolar ATPase membrane sector.
  Structure, 14, 1149-1156.  
16634087 H.Zheng, J.Zhao, W.Sheng, and X.Q.Xie (2006).
A transmembrane helix-bundle from G-protein coupled receptor CB2: biosynthesis, purification, and NMR characterization.
  Biopolymers, 83, 46-61.  
17215879 J.K.Rainey, L.Fliegel, and B.D.Sykes (2006).
Strategies for dealing with conformational sampling in structural calculations of flexible or kinked transmembrane peptides.
  Biochem Cell Biol, 84, 918-929.  
16730323 J.Weber (2006).
ATP synthase: subunit-subunit interactions in the stator stalk.
  Biochim Biophys Acta, 1757, 1162-1170.  
16971639 L.Balsalobre, A.Hernández-Madrid, D.Llull, A.J.Martín-Galiano, E.García, A.Fenoll, and la Campa (2006).
Molecular characterization of disease-associated streptococci of the mitis group that are optochin susceptible.
  J Clin Microbiol, 44, 4163-4171.  
17080295 M.Kobayashi, Y.Matsuki, I.Yumen, T.Fujiwara, and H.Akutsu (2006).
Signal assignment and secondary structure analysis of a uniformly [13C, 15N]-labeled membrane protein, H +-ATP synthase subunit c, by magic-angle spinning solid-state NMR.
  J Biomol NMR, 36, 279-293.  
16905113 M.R.Gunner, J.Mao, Y.Song, and J.Kim (2006).
Factors influencing the energetics of electron and proton transfers in proteins. What can be learned from calculations.
  Biochim Biophys Acta, 1757, 942-968.  
16607397 P.Dimroth, C.von Ballmoos, and T.Meier (2006).
Catalytic and mechanical cycles in F-ATP synthases. Fourth in the Cycles Review Series.
  EMBO Rep, 7, 276-282.  
16220142 A.E.Bednarski, S.C.Elgin, and H.B.Pakrasi (2005).
An inquiry into protein structure and genetic disease: introducing undergraduates to bioinformatics in a large introductory course.
  Cell Biol Educ, 4, 207-220.  
15863480 J.Khandogin, and C.L.Brooks (2005).
Constant pH molecular dynamics with proton tautomerism.
  Biophys J, 89, 141-157.  
16691471 T.Inoue, Y.Wang, K.Jefferies, J.Qi, A.Hinton, and M.Forgac (2005).
Structure and regulation of the V-ATPases.
  J Bioenerg Biomembr, 37, 393-398.  
15860619 T.Meier, P.Polzer, K.Diederichs, W.Welte, and P.Dimroth (2005).
Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus.
  Science, 308, 659-662.
PDB code: 1yce
15731457 T.P.Roosild, J.Greenwald, M.Vega, S.Castronovo, R.Riek, and S.Choe (2005).
NMR structure of Mistic, a membrane-integrating protein for membrane protein expression.
  Science, 307, 1317-1321.
PDB code: 1ygm
15860615 W.Junge, and N.Nelson (2005).
Structural biology. Nature's rotary electromotors.
  Science, 308, 642-644.  
16216877 Y.Wang, T.Inoue, and M.Forgac (2005).
Subunit a of the yeast V-ATPase participates in binding of bafilomycin.
  J Biol Chem, 280, 40481-40488.  
14990464 A.Aksimentiev, I.A.Balabin, R.H.Fillingame, and K.Schulten (2004).
Insights into the molecular mechanism of rotation in the Fo sector of ATP synthase.
  Biophys J, 86, 1332-1344.  
14970332 C.Ma, and G.Chang (2004).
Structure of the multidrug resistance efflux transporter EmrE from Escherichia coli.
  Proc Natl Acad Sci U S A, 101, 2852-2857.
PDB code: 1s7b
15255774 C.Mavroidis, A.Dubey, and M.L.Yarmush (2004).
Molecular machines.
  Annu Rev Biomed Eng, 6, 363-395.  
15180988 E.J.Bowman, L.A.Graham, T.H.Stevens, and B.J.Bowman (2004).
The bafilomycin/concanamycin binding site in subunit c of the V-ATPases from Neurospora crassa and Saccharomyces cerevisiae.
  J Biol Chem, 279, 33131-33138.  
15454418 J.Xing, H.Wang, C.von Ballmoos, P.Dimroth, and G.Oster (2004).
Torque generation by the Fo motor of the sodium ATPase.
  Biophys J, 87, 2148-2163.  
15247256 M.A.Treviño, M.F.García-Mayoral, P.Barral, M.Villalba, J.Santoro, M.Rico, R.Rodríguez, and M.Bruix (2004).
NMR solution structure of Ole e 6, a major allergen from olive tree pollen.
  J Biol Chem, 279, 39035-39041.
PDB code: 1ss3
15315950 M.Dittrich, S.Hayashi, and K.Schulten (2004).
ATP hydrolysis in the betaTP and betaDP catalytic sites of F1-ATPase.
  Biophys J, 87, 2954-2967.  
15103125 N.Numoto, A.Kita, and K.Miki (2004).
Structure of the C subunit of V-type ATPase from Thermus thermophilus at 1.85 A resolution.
  Acta Crystallogr D Biol Crystallogr, 60, 810-815.
PDB code: 1v9m
14691226 N.Sreerama, and R.W.Woody (2004).
On the analysis of membrane protein circular dichroism spectra.
  Protein Sci, 13, 100-112.  
15306026 P.Kemp, M.Gupta, and I.J.Molineux (2004).
Bacteriophage T7 DNA ejection into cells is initiated by an enzyme-like mechanism.
  Mol Microbiol, 53, 1251-1265.  
15001703 S.Zubkov, W.J.Lennarz, and S.Mohanty (2004).
Structural basis for the function of a minimembrane protein subunit of yeast oligosaccharyltransferase.
  Proc Natl Acad Sci U S A, 101, 3821-3826.
PDB code: 1rkl
15322078 Y.Wang, T.Inoue, and M.Forgac (2004).
TM2 but not TM4 of subunit c'' interacts with TM7 of subunit a of the yeast V-ATPase as defined by disulfide-mediated cross-linking.
  J Biol Chem, 279, 44628-44638.  
15024007 Z.Wang, D.B.Hicks, A.A.Guffanti, K.Baldwin, and T.A.Krulwich (2004).
Replacement of amino acid sequence features of a- and c-subunits of ATP synthases of Alkaliphilic Bacillus with the Bacillus consensus sequence results in defective oxidative phosphorylation and non-fermentative growth at pH 10.5.
  J Biol Chem, 279, 26546-26554.  
14506029 A.J.Martín-Galiano, L.Balsalobre, A.Fenoll, and la Campa (2003).
Genetic characterization of optochin-susceptible viridans group streptococci.
  Antimicrob Agents Chemother, 47, 3187-3194.  
12592029 B.D.Silverman (2003).
Hydrophobicity of transmembrane proteins: spatially profiling the distribution.
  Protein Sci, 12, 586-599.  
14645064 C.Kettner, A.Bertl, G.Obermeyer, C.Slayman, and H.Bihler (2003).
Electrophysiological analysis of the yeast V-type proton pump: variable coupling ratio and proton shunt.
  Biophys J, 85, 3730-3738.  
14595019 C.M.Angevine, K.A.Herold, and R.H.Fillingame (2003).
Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane.
  Proc Natl Acad Sci U S A, 100, 13179-13183.  
12473663 C.M.Angevine, and R.H.Fillingame (2003).
Aqueous access channels in subunit a of rotary ATP synthase.
  J Biol Chem, 278, 6066-6074.  
12624095 C.Mellwig, and B.Böttcher (2003).
A unique resting position of the ATP-synthase from chloroplasts.
  J Biol Chem, 278, 18544-18549.  
12525480 D.Zhang, and S.B.Vik (2003).
Close proximity of a cytoplasmic loop of subunit a with c subunits of the ATP synthase from Escherichia coli.
  J Biol Chem, 278, 12319-12324.  
14754233 H.Miki, M.Sato, and M.Kohmoto (2003).
Motion of a rotatory molecular motor and the chemical reaction rate.
  Phys Rev E Stat Nonlin Soft Matter Phys, 68, 061906.  
14656431 P.Dimroth, C.von Ballmoos, T.Meier, and G.Kaim (2003).
Electrical power fuels rotary ATP synthase.
  Structure, 11, 1469-1473.  
12917411 S.Kawasaki-Nishi, T.Nishi, and M.Forgac (2003).
Interacting helical surfaces of the transmembrane segments of subunits a and c' of the yeast V-ATPase defined by disulfide-mediated cross-linking.
  J Biol Chem, 278, 41908-41913.  
12482875 T.Nishi, S.Kawasaki-Nishi, and M.Forgac (2003).
The first putative transmembrane segment of subunit c" (Vma16p) of the yeast V-ATPase is not necessary for function.
  J Biol Chem, 278, 5821-5827.  
14581194 W.Im, M.Feig, and C.L.Brooks (2003).
An implicit membrane generalized born theory for the study of structure, stability, and interactions of membrane proteins.
  Biophys J, 85, 2900-2918.  
12019076 A.J.Martín-Galiano, B.Gorgojo, C.M.Kunin, and la Campa (2002).
Mefloquine and new related compounds target the F(0) complex of the F(0)F(1) H(+)-ATPase of Streptococcus pneumoniae.
  Antimicrob Agents Chemother, 46, 1680-1687.  
11925565 G.Manfredi, J.Fu, J.Ojaimi, J.E.Sadlock, J.Q.Kwong, J.Guy, and E.A.Schon (2002).
Rescue of a deficiency in ATP synthesis by transfer of MTATP6, a mitochondrial DNA-encoded gene, to the nucleus.
  Nat Genet, 30, 394-399.  
11956224 H.Mori, and K.Cline (2002).
A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid [Delta]pH/Tat translocase.
  J Cell Biol, 157, 205-210.  
12440697 H.Stahlberg, A.Engel, and A.Philippsen (2002).
Assessing the structure of membrane proteins: combining different methods gives the full picture.
  Biochem Cell Biol, 80, 563-568.  
11815621 I.Domgall, D.Venzke, U.Lüttge, R.Ratajczak, and B.Böttcher (2002).
Three-dimensional map of a plant V-ATPase based on electron microscopy.
  J Biol Chem, 277, 13115-13121.  
12429828 J.Ojaimi, J.Pan, S.Santra, W.J.Snell, and E.A.Schon (2002).
An algal nucleus-encoded subunit of mitochondrial ATP synthase rescues a defect in the analogous human mitochondrial-encoded subunit.
  Mol Biol Cell, 13, 3836-3844.  
11864990 J.Weber, S.Wilke-Mounts, and A.E.Senior (2002).
Quantitative determination of binding affinity of delta-subunit in Escherichia coli F1-ATPase: effects of mutation, Mg2+, and pH on Kd.
  J Biol Chem, 277, 18390-18396.  
12081500 J.Wei, Q.X.Tang, O.Varlamova, C.Roche, R.Lee, and T.S.Leyh (2002).
Cysteine biosynthetic enzymes are the pieces of a metabolic energy pump.
  Biochemistry, 41, 8493-8498.  
12357031 K.Nishio, A.Iwamoto-Kihara, A.Yamamoto, Y.Wada, and M.Futai (2002).
Subunit rotation of ATP synthase embedded in membranes: a or beta subunit rotation relative to the c subunit ring.
  Proc Natl Acad Sci U S A, 99, 13448-13452.  
11904412 L.Guan, F.D.Murphy, and H.R.Kaback (2002).
Surface-exposed positions in the transmembrane helices of the lactose permease of Escherichia coli determined by intermolecular thiol cross-linking.
  Proc Natl Acad Sci U S A, 99, 3475-3480.  
11952801 P.Turina, and B.A.Melandri (2002).
A point mutation in the ATP synthase of Rhodobacter capsulatus results in differential contributions of Delta(pH) and Delta(phi) in driving the ATP synthesis reaction.
  Eur J Biochem, 269, 1984-1992.  
11952796 U.Matthey, D.Braun, and P.Dimroth (2002).
NMR investigations of subunit c of the ATP synthase from Propionigenium modestum in chloroform/methanol/water (4 : 4 : 1).
  Eur J Biochem, 269, 1942-1946.  
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 la Campa (2001).
The promoter of the operon encoding the F0F1 ATPase of Streptococcus pneumoniae is inducible by pH.
  Mol Microbiol, 41, 1327-1338.  
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.  
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.  
11226225 F.X.Zhou, H.J.Merianos, A.T.Brunger, and D.M.Engelman (2001).
Polar residues drive association of polyleucine transmembrane helices.
  Proc Natl Acad Sci U S A, 98, 2250-2255.  
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.  
11309597 M.J.Schnitzer (2001).
Molecular motors. Doing a rotary two-step.
  Nature, 410, 878.  
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.  
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.  
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.  
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.  
11101285 H.Yerushalmi, and S.Schuldiner (2000).
A model for coupling of H(+) and substrate fluxes based on "time-sharing" of a common binding site.
  Biochemistry, 39, 14711-14719.  
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.  
11169921 J.le Coutre, and H.K.Kaback (2000).
Structure-function relationships of integral membrane proteins: membrane transporters vs channels.
  Biopolymers, 55, 297-307.  
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.  
10827963 M.Grabe, H.Wang, and G.Oster (2000).
The mechanochemistry of V-ATPase proton pumps.
  Biophys J, 78, 2798-2813.  
10858302 M.Harrison, B.Powell, M.E.Finbow, and J.B.Findlay (2000).
Identification of lipid-accessible sites on the nephrops 16-kDa proteolipid incorporated into a hybrid vacuolar H(+)-ATPase: site-directed labeling with N-(1-Pyrenyl)cyclohexylcarbodiimide and fluorescence quenching analysis.
  Biochemistry, 39, 7531-7537.  
10753949 P.C.Jones, J.Hermolin, and R.H.Fillingame (2000).
Mutations in single hairpin units of genetically fused subunit c provide support for a rotary catalytic mechanism in F(0)F(1) ATP synthase.
  J Biol Chem, 275, 11355-11360.  
10978147 P.Venkatesan, I.Kwaw, Y.Hu, and H.R.Kaback (2000).
Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: helix VII.
  Biochemistry, 39, 10641-10648.  
10978149 P.Venkatesan, Y.Hu, and H.R.Kaback (2000).
Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: helix X.
  Biochemistry, 39, 10656-10661.  
10978148 P.Venkatesan, Z.Liu, Y.Hu, and H.R.Kaback (2000).
Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: N-ethylmaleimide-sensitive face of helix II.
  Biochemistry, 39, 10649-10655.  
11031230 R.E.Dalbey, and A.Kuhn (2000).
Evolutionarily related insertion pathways of bacterial, mitochondrial, and thylakoid membrane proteins.
  Annu Rev Cell Dev Biol, 16, 51-87.  
11015191 R.M.Taylor, S.D.Zakharov, J.Bernard Heymann, M.E.Girvin, and W.A.Cramer (2000).
Folded state of the integral membrane colicin E1 immunity protein in solvents of mixed polarity.
  Biochemistry, 39, 12131-12139.  
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.  
10924155 S.Nadanaciva, J.Weber, and A.E.Senior (2000).
New probes of the F1-ATPase catalytic transition state reveal that two of the three catalytic sites can assume a transition state conformation simultaneously.
  Biochemistry, 39, 9583-9590.  
11004441 T.Bizouarn, J.Meuller, M.Axelsson, and J.Rydström (2000).
The transmembrane domain and the proton channel in proton-pumping transhydrogenases.
  Biochim Biophys Acta, 1459, 284-290.  
11087408 W.Zhang, and H.R.Kaback (2000).
Effect of the lipid phase transition on the lactose permease from Escherichia coli.
  Biochemistry, 39, 14538-14542.  
10899118 Y.Asai, I.Kawagishi, R.E.Sockett, and M.Homma (2000).
Coupling ion specificity of chimeras between H(+)- and Na(+)-driven motor proteins, MotB and PomB, in Vibrio polar flagella.
  EMBO J, 19, 3639-3648.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.