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PDBsum entry 3acp
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References listed in PDB file
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Key reference
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Title
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Crystal structure of yeast rpn14, A chaperone of the 19 s regulatory particle of the proteasome.
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Authors
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S.Kim,
Y.Saeki,
K.Fukunaga,
A.Suzuki,
K.Takagi,
T.Yamane,
K.Tanaka,
T.Mizushima,
K.Kato.
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Ref.
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J Biol Chem, 2010,
285,
15159-15166.
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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 ubiquitin-proteasome pathway is a major proteolytic system in eukaryotic
cells and regulates various cellular processes. The 26 S proteasome, the central
enzyme of this pathway, consists of a proteolytic core particle and two 19 S
regulatory particles (RPs) composed of ATPase (Rpt) and non-ATPase (Rpn)
subunits. Growing evidence indicates that proteasome assembly is assisted by a
variety of chaperones. In particular, it has been reported recently that Nas2,
Nas6, Rpn14, and Hsm3 bind specific Rpt subunits, thereby contributing to the
formation of 19 S RP. Rpn14 transiently binds to the C-terminal domain of the
Rpt6 subunit (Rpt6-C) during maturation of the ATPase ring of 19 S RP. In this
study, we determined the crystal structure of yeast Rpn14 at 2.0 A resolution,
which revealed that this chaperone consists of a unique N-terminal domain with
unknown function and a C-terminal domain assuming a canonical seven-bladed
beta-propeller fold. The Rpt6-binding site on Rpn14 was predicted based on
structural comparison with the complex formed between Nas6 and Rpt3-C. The top
face of Rpn14 exhibits a highly acidic surface area, whereas the putative
interacting surface of Rpt6-C is basic. By inspection of structural data along
with genetic and biochemical data, we determined the specific residues of Rpn14
and Rpt6 for complementary charge interactions that are required for 19 S RP
assembly.
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