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PDBsum entry 5mp9
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Contents |
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241 a.a.
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250 a.a.
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244 a.a.
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240 a.a.
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242 a.a.
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231 a.a.
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243 a.a.
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196 a.a.
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226 a.a.
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204 a.a.
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195 a.a.
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212 a.a.
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222 a.a.
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232 a.a.
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390 a.a.
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385 a.a.
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389 a.a.
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388 a.a.
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381 a.a.
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386 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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Structural insights into the functional cycle of the atpase module of the 26s proteasome.
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Authors
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M.Wehmer,
T.Rudack,
F.Beck,
A.Aufderheide,
G.Pfeifer,
J.M.Plitzko,
F.Förster,
K.Schulten,
W.Baumeister,
E.Sakata.
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Ref.
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Proc Natl Acad Sci U S A, 2017,
114,
1305-1310.
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PubMed id
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Abstract
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In eukaryotic cells, the ubiquitin-proteasome system (UPS) is responsible for
the regulated degradation of intracellular proteins. The 26S holocomplex
comprises the core particle (CP), where proteolysis takes place, and one or two
regulatory particles (RPs). The base of the RP is formed by a heterohexameric
AAA(+) ATPase module, which unfolds and translocates substrates into the CP.
Applying single-particle cryo-electron microscopy (cryo-EM) and image
classification to samples in the presence of different nucleotides and
nucleotide analogs, we were able to observe four distinct conformational states
(s1 to s4). The resolution of the four conformers allowed for the construction
of atomic models of the AAA(+) ATPase module as it progresses through the
functional cycle. In a hitherto unobserved state (s4), the gate controlling
access to the CP is open. The structures described in this study allow us to put
forward a model for the 26S functional cycle driven by ATP hydrolysis.
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