1n57: Difference between revisions

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[[Image:1n57.gif|left|200px]]
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{{STRUCTURE_1n57|  PDB=1n57  |  SCENE=  }}  
{{STRUCTURE_1n57|  PDB=1n57  |  SCENE=  }}  


'''Crystal Structure of Chaperone Hsp31'''
===Crystal Structure of Chaperone Hsp31===




==Overview==
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Heat shock proteins (Hsps) play essential protective roles under stress conditions by preventing the formation of protein aggregates and degrading misfolded proteins. EcHsp31, the yedU (hchA) gene product, is a representative member of a family of chaperones that alleviates protein misfolding by interacting with early unfolding intermediates. The 1.6-A crystal structure of the EcHsp31 dimer reveals a system of hydrophobic patches, canyons, and grooves, which may stabilize partially unfolded substrate. The presence of a well conserved, yet buried, triad in each two-domain subunit suggests a still unproven hydrolytic function of the protein. A flexible extended linker between the A and P domains may play a role in conformational flexibility and substrate binding. The alpha-beta sandwich of the EcHsp31 monomer shows structural similarity to PhPI, a protease belonging to the DJ-1 superfamily. The structure-guided sequence alignment indicates that Hsp31 homologs can be divided in three classes based on variations in the P domain that dramatically affect both oligomerization and catalytic triad formation.
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{{ABSTRACT_PUBMED_12621151}}


==About this Structure==
==About this Structure==
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[[Category: Quigley, P M.]]
[[Category: Quigley, P M.]]
[[Category: Alpha-beta sandwich]]
[[Category: Alpha-beta sandwich]]
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Revision as of 16:34, 28 July 2008

File:1n57.png

Template:STRUCTURE 1n57

Crystal Structure of Chaperone Hsp31

Template:ABSTRACT PUBMED 12621151

About this Structure

1N57 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad., Quigley PM, Korotkov K, Baneyx F, Hol WG, Proc Natl Acad Sci U S A. 2003 Mar 18;100(6):3137-42. Epub 2003 Mar 5. PMID:12621151

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