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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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References listed in PDB file
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Key reference
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Title
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The structure of the membrane extrinsic region of bovine ATP synthase.
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Authors
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D.M.Rees,
A.G.Leslie,
J.E.Walker.
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Ref.
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Proc Natl Acad Sci U S A, 2009,
106,
21597-21601.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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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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