2b26
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= SIS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), Hsc70-2, Hsc2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster]) | |GENE= SIS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), Hsc70-2, Hsc2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b26 OCA], [http://www.ebi.ac.uk/pdbsum/2b26 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b26 RCSB]</span> | ||
}} | }} | ||
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[[Category: hsp40 sis1 hsp70 ssa1]] | [[Category: hsp40 sis1 hsp70 ssa1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:00:28 2008'' |
Revision as of 23:00, 30 March 2008
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| , resolution 3.2Å | |||||||
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| Gene: | SIS1 (Saccharomyces cerevisiae), Hsc70-2, Hsc2 (Drosophila melanogaster) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
2B26 is a Protein complex structure of sequences from Drosophila melanogaster and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
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
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