1xao
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(New page: 200px<br /><applet load="1xao" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xao, resolution 2.07Å" /> '''Hsp40-Ydj1 dimerizat...)
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Revision as of 03:49, 21 November 2007
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Hsp40-Ydj1 dimerization domain
Overview
The molecular chaperone Hsp40 functions as a dimer. The dimer formation is, critical for Hsp40 molecular chaperone activity to facilitate Hsp70 to, refold non-native polypeptides. We have determined the crystal structure, of the C-terminal fragment of yeast Hsp40 Ydj1 that is responsible for, Ydj1 dimerization by MAD method. The C-terminal fragment of Ydj1 comprises, of the domain III of Ydj1 and the Ydj1 C-terminal dimerization motif. The, crystal structure indicates that the dimerization motif of type I Hsp40, Ydj1 differs significantly from that of yeast type II Hsp40. The C, terminus of type I Hsp40 Ydj1 from one monomer forms beta-strands with the, domain III from the other monomer in the homo-dimer. The L372 from Ydj1 C, terminus inserts its side-chain into a hydrophobic pocket on domain III., The modeled full-length Ydj1 dimer structure reveals that a large cleft is, formed between the two monomers. The domain IIs of Ydj1 monomers that, contain the zinc-finger motifs points directly against each other.
About this Structure
1XAO is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 reveals novel dimerization motif for Hsp40., Wu Y, Li J, Jin Z, Fu Z, Sha B, J Mol Biol. 2005 Mar 4;346(4):1005-11. Epub 2005 Jan 16. PMID:15701512
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