2b26
From Proteopedia
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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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