2b26: Difference between revisions

Revision as of 10:52, 28 July 2008

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File:2b26.png

Template:STRUCTURE 2b26

The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1

Template:ABSTRACT PUBMED 16737444

About this StructureAbout this Structure

2B26 is a Protein complex structure of sequences from Drosophila melanogaster and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of yeast Sis1 peptide-binding fragment and Hsp70 Ssa1 C-terminal complex., Li J, Wu Y, Qian X, Sha B, Biochem J. 2006 Sep 15;398(3):353-60. PMID:16737444

Page seeded by OCA on Mon Jul 28 10:52:41 2008

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OCA

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-'''The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1'''
+===The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1===
-==Overview==
+<!--
-Heat shock protein (Hsp) 40 facilitates the critical role of Hsp70 in a number of cellular processes such as protein folding, assembly, degradation and translocation in vivo. Hsp40 and Hsp70 stay in close contact to achieve these diverse functions. The conserved C-terminal EEVD motif in Hsp70 has been shown to regulate Hsp40-Hsp70 interaction by an unknown mechanism. Here, we provide a structural basis for this regulation by determining the crystal structure of yeast Hsp40 Sis1 peptide-binding fragment complexed with the Hsp70 Ssa1 C-terminal. The Ssa1 extreme C-terminal eight residues, G634PTVEEVD641, form a beta-strand with the domain I of Sis1 peptide-binding fragment. Surprisingly, the Ssa1 C-terminal binds Sis1 at the site where Sis1 interacts with the non-native polypeptides. The negatively charged residues within the EEVD motif in Ssa1 C-terminal form extensive charge-charge interactions with the positively charged residues in Sis1. The structure-based mutagenesis data support the structural observations.
+The line below this paragraph, {{ABSTRACT_PUBMED_16737444}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16737444 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16737444}}
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 [[Category: Wu, Y.]]
 [[Category: Hsp40 sis1 hsp70 ssa1]]
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