PDBsum entry 1fx0

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protein Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
477 a.a. *
467 a.a. *
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Crystal structure of the chloroplast f1-atpase from spinach
Structure: Atp synthase alpha chain. Chain: a. Atp synthase beta chain. Chain: b. Ec:
Source: Spinacia oleracea. Spinach. Organism_taxid: 3562. Organism_taxid: 3562
Biol. unit: Hexamer (from PDB file)
3.20Å     R-factor:   0.319     R-free:   0.350
Authors: G.Groth,E.Pohl
Key ref:
G.Groth and E.Pohl (2001). The structure of the chloroplast F1-ATPase at 3.2 A resolution. J Biol Chem, 276, 1345-1352. PubMed id: 11032839 DOI: 10.1074/jbc.M008015200
25-Sep-00     Release date:   25-Sep-01    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P06450  (ATPA_SPIOL) -  ATP synthase subunit alpha, chloroplastic
507 a.a.
477 a.a.
Protein chain
Pfam   ArchSchema ?
P00825  (ATPB_SPIOL) -  ATP synthase subunit beta, chloroplastic
498 a.a.
467 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.  - H(+)-transporting two-sector ATPase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O + H+(In) = ADP + phosphate + H+(Out)
+ H(2)O
+ H(+)(In)
+ 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   7 terms 
  Biological process     transport   7 terms 
  Biochemical function     nucleotide binding     7 terms  


DOI no: 10.1074/jbc.M008015200 J Biol Chem 276:1345-1352 (2001)
PubMed id: 11032839  
The structure of the chloroplast F1-ATPase at 3.2 A resolution.
G.Groth, E.Pohl.
The structure of the F(1)-ATPase from spinach chloroplasts was determined to 3.2 A resolution by molecular replacement based on the homologous structure of the bovine mitochondrial enzyme. The crystallized complex contains four different subunits in a stoichiometry of alpha(3)beta(3)gammaepsilon. Subunit delta was removed before crystallization to improve the diffraction of the crystals. The overall structure of the noncatalytic alpha-subunits and the catalytic beta-subunits is highly similar to those of the mitochondrial and thermophilic subunits. However, in the crystal structure of the chloroplast enzyme, all alpha- and beta-subunits adopt a closed conformation and appear to contain no bound adenine nucleotides. The superimposed crystallographic symmetry in the space group R32 impaired an exact tracing of the gamma- and epsilon-subunits in the complex. However, clear electron density was present at the core of the alpha(3)beta(3)-subcomplex, which probably represents the C-terminal domain of the gamma-subunit. The structure of the spinach chloroplast F(1) has a potential binding site for the phytotoxin, tentoxin, at the alphabeta-interface near betaAsp(83) and an insertion from betaGly(56)-Asn(60) in the N-terminal beta-barrel domain probably increases the thermal stability of the complex. The structure probably represents an inactive latent state of the ATPase, which is unique to chloroplast and cyanobacterial enzymes.
  Selected figure(s)  
Figure 5.
Fig. 5. Schematic representation of the N-terminal six-stranded -barrel domain of the -subunit in the mitochondrial (A), chloroplast (B), and thermophilic ATPase (C).
Figure 7.
Fig. 7. Suggested potential Tentoxin binding site of the chloroplast ATPase (A) and corresponding domains in the mitochondrial (B) and thermophilic F[1] complex (C). Surface representation of residues within 20.0 Å of the essential Asp83 in CF[1] and the corresponding residues Asp67 in MF[1] and Asp68 in TF[1]. Structures are shown in stereo view with the crystallographic axis in the vertical position as they would appear from the outside of the [3] [3] complex.
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2001, 276, 1345-1352) copyright 2001.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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.
  Biophys J, 98, 434-442.  
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
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.  
18377232 P.Schürmann, and B.B.Buchanan (2008).
The ferredoxin/thioredoxin system of oxygenic photosynthesis.
  Antioxid Redox Signal, 10, 1235-1274.  
19052322 S.Hong, and P.L.Pedersen (2008).
ATP synthase and the actions of inhibitors utilized to study its roles in human health, disease, and other scientific areas.
  Microbiol Mol Biol Rev, 72, 590.  
16832703 G.del Riego, L.M.Casano, M.Martín, and B.Sabater (2006).
Multiple phosphorylation sites in the beta subunit of thylakoid ATP synthase.
  Photosynth Res, 89, 11-18.  
17082766 V.Kabaleeswaran, N.Puri, J.E.Walker, A.G.Leslie, and D.M.Mueller (2006).
Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase.
  EMBO J, 25, 5433-5442.
PDB code: 2hld
16691485 M.L.Richter, H.S.Samra, F.He, A.J.Giessel, and K.K.Kuczera (2005).
Coupling proton movement to ATP synthesis in the chloroplast ATP synthase.
  J Bioenerg Biomembr, 37, 467-473.  
15272171 D.M.Mueller, N.Puri, V.Kabaleeswaran, C.Terry, A.G.Leslie, and J.E.Walker (2004).
Crystallization and preliminary crystallographic studies of the mitochondrial F1-ATPase from the yeast Saccharomyces cerevisiae.
  Acta Crystallogr D Biol Crystallogr, 60, 1441-1444.  
15006644 M.O.Souza, T.B.Creczynski-Pasa, H.M.Scofano, P.Gräber, and J.A.Mignaco (2004).
High hydrostatic pressure perturbs the interactions between CF(0)F(1) subunits and induces a dual effect on activity.
  Int J Biochem Cell Biol, 36, 920-930.  
14633978 J.L.Rubinstein, J.E.Walker, and R.Henderson (2003).
Structure of the mitochondrial ATP synthase by electron cryomicroscopy.
  EMBO J, 22, 6182-6192.  
12944266 R.A.Böckmann, and H.Grubmüller (2003).
Conformational dynamics of the F1-ATPase beta-subunit: a molecular dynamics study.
  Biophys J, 85, 1482-1491.  
12360520 C.Minoletti, J.Santolini, F.Haraux, J.Pothier, and F.André (2002).
Rebuilt 3D structure of the chloroplast f1 ATPase-tentoxin complex.
  Proteins, 49, 302-320.  
12423357 C.von Ballmoos, T.Meier, and P.Dimroth (2002).
Membrane embedded location of Na+ or H+ binding sites on the rotor ring of F1F0 ATP synthases.
  Eur J Biochem, 269, 5581-5589.  
11904410 G.Groth (2002).
Structure of spinach chloroplast F1-ATPase complexed with the phytopathogenic inhibitor tentoxin.
  Proc Natl Acad Sci U S A, 99, 3464-3468.
PDB code: 1kmh
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 code is shown on the right.