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PDBsum entry 2wss

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2wss
Jmol
Contents
Protein chains
510 a.a. *
480 a.a. *
(+ 0 more) 467 a.a. *
260 a.a. *
131 a.a. *
47 a.a. *
167 a.a. *
86 a.a. *
28 a.a. *
66 a.a. *
146 a.a. *
41 a.a. *
17 a.a. *
Ligands
ANP ×8
ADP ×2
Metals
_MG ×10
* Residue conservation analysis
PDB id:
2wss
Name: Hydrolase
Title: The structure of the membrane extrinsic region of bovine atp synthase
Structure: Atp synthase subunit alpha, mitochondrial. Chain: a, b, c, j, k, l. Atp synthase subunit beta, mitochondrial. Chain: d, e, f, m, n, o. Fragment: residues 47-528. Atp synthase subunit gamma, mitochondrial. Chain: g, p. Fragment: heart isoform, residues 26-297. Synonym: f-atpase gamma subunit.
Source: Bos taurus. Bovine. Organism_taxid: 9913. Synthetic: yes. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
3.20Å     R-factor:   0.220     R-free:   0.271
Authors: D.M.Rees,A.G.W.Leslie,J.E.Walker
Key ref: D.M.Rees et al. (2009). The structure of the membrane extrinsic region of bovine ATP synthase. Proc Natl Acad Sci U S A, 106, 21597-21601. PubMed id: 19995987
Date:
09-Sep-09     Release date:   17-Nov-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P19483  (ATPA_BOVIN) -  ATP synthase subunit alpha, mitochondrial
Seq:
Struc:
 
Seq:
Struc:
553 a.a.
510 a.a.*
Protein chains
Pfam   ArchSchema ?
P19483  (ATPA_BOVIN) -  ATP synthase subunit alpha, mitochondrial
Seq:
Struc:
 
Seq:
Struc:
553 a.a.
480 a.a.*
Protein chains
Pfam   ArchSchema ?
P00829  (ATPB_BOVIN) -  ATP synthase subunit beta, mitochondrial
Seq:
Struc:
 
Seq:
Struc:
528 a.a.
467 a.a.
Protein chains
Pfam   ArchSchema ?
P05631  (ATPG_BOVIN) -  ATP synthase subunit gamma, mitochondrial
Seq:
Struc:
298 a.a.
260 a.a.
Protein chains
No UniProt id for this chain
Struc: 131 a.a.
Protein chains
Pfam   ArchSchema ?
P05632  (ATP5E_BOVIN) -  ATP synthase subunit epsilon, mitochondrial
Seq:
Struc:
51 a.a.
47 a.a.
Protein chain
No UniProt id for this chain
Struc: 167 a.a.
Protein chain
Pfam   ArchSchema ?
P13619  (AT5F1_BOVIN) -  ATP synthase F(0) complex subunit B1, mitochondrial
Seq:
Struc:
256 a.a.
86 a.a.
Protein chain
No UniProt id for this chain
Struc: 28 a.a.
Protein chain
Pfam   ArchSchema ?
P02721  (ATP5J_BOVIN) -  ATP synthase-coupling factor 6, mitochondrial
Seq:
Struc:
108 a.a.
66 a.a.
Protein chain
Pfam   ArchSchema ?
P13621  (ATPO_BOVIN) -  ATP synthase subunit O, mitochondrial
Seq:
Struc:
213 a.a.
146 a.a.*
Protein chain
No UniProt id for this chain
Struc: 41 a.a.
Protein chain
Pfam   ArchSchema ?
P02721  (ATP5J_BOVIN) -  ATP synthase-coupling factor 6, mitochondrial
Seq:
Struc:
108 a.a.
17 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   14 terms 
  Biological process     transport   13 terms 
  Biochemical function     nucleotide binding     11 terms  

 

 
Proc Natl Acad Sci U S A 106:21597-21601 (2009)
PubMed id: 19995987  
 
 
The structure of the membrane extrinsic region of bovine ATP synthase.
D.M.Rees, A.G.Leslie, J.E.Walker.
 
  ABSTRACT  
 
The structure of the complex between bovine mitochondrial F(1)-ATPase and a stator subcomplex has been determined at a resolution of 3.2 A. The resolved region of the stator contains residues 122-207 of subunit b; residues 5-25 and 35-57 of F(6); 3 segments of subunit d from residues 30-40, 65-74, and 85-91; and residues 1-146 and 169-189 of the oligomycin sensitivity conferral protein (OSCP). The stator subcomplex represents its membrane distal part, and its structure has been augmented with an earlier structure of a subcomplex containing residues 79-183, 3-123, and 5-70 of subunits b, d, and F(6), respectively, which extends to the surface of the inner membrane of the mitochondrion. The N-terminal domain of the OSCP links the stator with F(1)-ATPase via alpha-helical interactions with the N-terminal region of subunit alpha(E). Its C-terminal domain makes extensive helix-helix interactions with the C-terminal alpha-helix of subunit b from residues 190-207. Subunit b extends as a continuous 160-A long alpha-helix from residue 188 back to residue 79 near to the surface of the inner mitochondrial membrane. This helix appears to be stiffened by other alpha-helices in subunits d and F(6), but the structure can bend inward toward the F(1) domain around residue 146 of subunit b. The linker region between the 2 domains of the OSCP also appears to be flexible, enabling the stator to adjust its shape as it passes over the changing profile of the F(1) domain during a catalytic cycle. The structure of the membrane extrinsic part of bovine ATP synthase is now complete.
 

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
21368147 A.Wächter, Y.Bi, S.D.Dunn, B.D.Cain, H.Sielaff, F.Wintermann, S.Engelbrecht, and W.Junge (2011).
Two rotary motors in F-ATP synthase are elastically coupled by a flexible rotor and a stiff stator stalk.
  Proc Natl Acad Sci U S A, 108, 3924-3929.  
21481781 K.Okazaki, and S.Takada (2011).
Structural comparison of F1-ATPase: interplay among enzyme structures, catalysis, and rotations.
  Structure, 19, 588-598.  
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.
  Proc Natl Acad Sci U S A, 107, 16823-16827.
PDB code: 2xnd
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.