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| {{STRUCTURE_2b26| PDB=2b26 | SCENE= }} | | {{STRUCTURE_2b26| PDB=2b26 | SCENE= }} |
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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=== |
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| ==Overview==
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| 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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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Wu, Y.]] | | [[Category: Wu, Y.]] |
| [[Category: Hsp40 sis1 hsp70 ssa1]] | | [[Category: Hsp40 sis1 hsp70 ssa1]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:45:36 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:52:41 2008'' |
