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PDBsum entry 3acp
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Chaperone
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Title:
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Crystal structure of yeast rpn14, a chaperone of the 19s regulatory particle of the proteasome
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Structure:
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Wd repeat-containing protein ygl004c. Chain: a. Synonym: wd40 protein. Engineered: yes
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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2.00Å
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R-factor:
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0.203
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R-free:
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0.255
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Authors:
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S.Kim,Y.Saeki,A.Suzuki,K.Takagi,K.Fukunaga,T.Yamane,K.Kato,K.Tanaka, T.Mizushima
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Key ref:
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S.Kim
et al.
(2010).
Crystal structure of yeast rpn14, a chaperone of the 19 S regulatory particle of the proteasome.
J Biol Chem,
285,
15159-15166.
PubMed id:
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Date:
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08-Jan-10
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Release date:
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16-Mar-10
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PROCHECK
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Headers
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References
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P53196
(RPN14_YEAST) -
26S proteasome regulatory subunit RPN14 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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417 a.a.
417 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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J Biol Chem
285:15159-15166
(2010)
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PubMed id:
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Crystal structure of yeast rpn14, a chaperone of the 19 S regulatory particle of the proteasome.
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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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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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Links
