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PDBsum entry 2wss
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Contents |
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510 a.a.
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480 a.a.
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(+ 0 more)
467 a.a.
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260 a.a.
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131 a.a.
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47 a.a.
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167 a.a.
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86 a.a.
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28 a.a.
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66 a.a.
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146 a.a.
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41 a.a.
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17 a.a.
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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The structure of the membrane extrinsic region of bovine atp synthase
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Structure:
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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.
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Source:
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Bos taurus. Bovine. Organism_taxid: 9913. Synthetic: yes. Expressed in: escherichia coli. Expression_system_taxid: 511693.
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Resolution:
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3.20Å
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R-factor:
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0.220
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R-free:
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0.271
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Authors:
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D.M.Rees,A.G.W.Leslie,J.E.Walker
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Key ref:
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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:
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Date:
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09-Sep-09
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Release date:
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17-Nov-09
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PROCHECK
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Headers
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References
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P19483
(ATPA_BOVIN) -
ATP synthase subunit alpha, mitochondrial from Bos taurus
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Seq:
Struc:
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553 a.a.
510 a.a.*
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P19483
(ATPA_BOVIN) -
ATP synthase subunit alpha, mitochondrial from Bos taurus
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Seq:
Struc:
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553 a.a.
480 a.a.*
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P00829
(ATPB_BOVIN) -
ATP synthase subunit beta, mitochondrial from Bos taurus
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Seq:
Struc:
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528 a.a.
467 a.a.
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P05631
(ATPG_BOVIN) -
ATP synthase subunit gamma, mitochondrial from Bos taurus
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Seq:
Struc:
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298 a.a.
260 a.a.
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P05630
(ATPD_BOVIN) -
ATP synthase subunit delta, mitochondrial from Bos taurus
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Seq:
Struc:
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168 a.a.
131 a.a.
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P05632
(ATP5E_BOVIN) -
ATP synthase subunit epsilon, mitochondrial from Bos taurus
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Seq:
Struc:
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51 a.a.
47 a.a.
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P13621
(ATPO_BOVIN) -
ATP synthase subunit O, mitochondrial from Bos taurus
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Seq:
Struc:
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213 a.a.
167 a.a.*
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P13619
(AT5F1_BOVIN) -
ATP synthase F(0) complex subunit B1, mitochondrial from Bos taurus
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Seq:
Struc:
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256 a.a.
86 a.a.
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P13620
(ATP5H_BOVIN) -
ATP synthase subunit d, mitochondrial from Bos taurus
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Seq:
Struc:
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161 a.a.
28 a.a.
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P02721
(ATP5J_BOVIN) -
ATP synthase-coupling factor 6, mitochondrial from Bos taurus
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Seq:
Struc:
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108 a.a.
66 a.a.
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P13621
(ATPO_BOVIN) -
ATP synthase subunit O, mitochondrial from Bos taurus
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Seq:
Struc:
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213 a.a.
146 a.a.*
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Enzyme class:
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Chains D, E, F, M, N, O:
E.C.7.1.2.2
- H(+)-transporting two-sector ATPase.
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Reaction:
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ATP + H2O + 4 H+(in) = ADP + phosphate + 5 H+(out)
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ATP
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+
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H2O
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+
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4
×
H(+)(in)
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=
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ADP
Bound ligand (Het Group name = )
corresponds exactly
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phosphate
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+
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5
×
H(+)(out)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Proc Natl Acad Sci U S A
106:21597-21601
(2009)
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PubMed id:
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The structure of the membrane extrinsic region of bovine ATP synthase.
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D.M.Rees,
A.G.Leslie,
J.E.Walker.
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ABSTRACT
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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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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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.
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Nat Struct Mol Biol,
19,
485.
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PDB codes:
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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.
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Proc Natl Acad Sci U S A,
108,
3924-3929.
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K.Okazaki,
and
S.Takada
(2011).
Structural comparison of F1-ATPase: interplay among enzyme structures, catalysis, and rotations.
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Structure,
19,
588-598.
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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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Proc Natl Acad Sci U S A,
107,
16823-16827.
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PDB code:
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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.
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Links
