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PDBsum entry 1ya7
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Hydrolase/hydrolase activator
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PDB id
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1ya7
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Contents |
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(+ 1 more)
227 a.a.
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(+ 1 more)
203 a.a.
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(+ 1 more)
218 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 1.9 a structure of a proteasome-11s activator complex and implications for proteasome-Pan/pa700 interactions.
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Authors
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A.Förster,
E.I.Masters,
F.G.Whitby,
H.Robinson,
C.P.Hill.
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Ref.
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Mol Cell, 2005,
18,
589-599.
[DOI no: ]
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PubMed id
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Abstract
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Proteasomes are cylindrical structures that function in multiple cellular
processes by degrading a wide variety of cytosolic and nuclear proteins.
Substrate access and product release from the enclosed catalytic chamber occurs
through axial pores that are opened by activator complexes. Here, we report
high-resolution structures of wild-type and mutant archaeal proteasomes bound to
the activator PA26. These structures support the proposal that an ordered open
conformation is required for proteolysis and that its formation can be triggered
by outward displacement of surrounding residues. The structures and associated
biochemical assays reveal the mechanism of binding, which involves an
interaction between the PA26 C terminus and a conserved lysine. Surprisingly,
biochemical observations implicate an equivalent interaction for the unrelated
ATP-dependent activators PAN and PA700.
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Figure 4.
Figure 4. Pore Conformation
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Figure 5.
Figure 5. PA26-Proteasome Interaction
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2005,
18,
589-599)
copyright 2005.
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