1nlt
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(New page: 200px<br /><applet load="1nlt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nlt, resolution 2.70Å" /> '''The crystal structur...)
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Revision as of 20:15, 20 November 2007
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The crystal structure of Hsp40 Ydj1
Overview
The mechanisms by which Hsp40 functions as a molecular chaperone to, recognize and bind non-native polypeptides is not understood. We have, identified a peptide substrate for Ydj1, a member of the type I Hsp40 from, yeast. The structure of the Ydj1 peptide binding fragment and its peptide, substrate complex was determined to 2.7 A resolution. The complex, structure reveals that Ydj1 peptide binding fragment forms an L-shaped, molecule constituted by three domains. The domain I exhibits a similar, protein folds as domain III while the domain II contains two Zinc finger, motifs. The peptide substrate binds Ydj1 by forming an extra beta strand, with domain I of Ydj1. The Leucine residue in the middle of the peptide, substrate GWLYEIS inserts its side chain into a hydrophobic pocket formed, on the molecular surface of Ydj1 domain I. The Zinc finger motifs located, in the Ydj1 domain II are not in the vicinity of peptide substrate binding, site.
About this Structure
1NLT is a Single protein structure of sequence from Saccharomyces cerevisiae with ZN as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate., Li J, Qian X, Sha B, Structure. 2003 Dec;11(12):1475-83. PMID:14656432
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