2o1w: Difference between revisions

Revision as of 17:19, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2o1w.png

Template:STRUCTURE 2o1w

Structure of N-terminal plus middle domains (N+M) of GRP94Structure of N-terminal plus middle domains (N+M) of GRP94

Template:ABSTRACT PUBMED 17936703

About this StructureAbout this Structure

2O1W is a Single protein structure of sequence from Canis lupus familiaris. Full crystallographic information is available from OCA.

ReferenceReference

Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones., Dollins DE, Warren JJ, Immormino RM, Gewirth DT, Mol Cell. 2007 Oct 12;28(1):41-56. PMID:17936703

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-'''Structure of N-terminal plus middle domains (N+M) of GRP94'''
+===Structure of N-terminal plus middle domains (N+M) of GRP94===
-==Overview==
+<!--
-GRP94, an essential endoplasmic reticulum chaperone, is required for the conformational maturation of proteins destined for cell-surface display or export. The extent to which GRP94 and its cytosolic paralog, Hsp90, share a common mechanism remains controversial. GRP94 has not been shown conclusively to hydrolyze ATP or bind cochaperones, and both activities, by contrast, result in conformational changes and N-terminal dimerization in Hsp90 that are critical for its function. Here, we report the 2.4 A crystal structure of mammalian GRP94 in complex with AMPPNP and ADP. The chaperone is conformationally insensitive to the identity of the bound nucleotide, adopting a "twisted V" conformation that precludes N-terminal domain dimerization. We also present conclusive evidence that GRP94 possesses ATPase activity. Our observations provide a structural explanation for GRP94's observed rate of ATP hydrolysis and suggest a model for the role of ATP binding and hydrolysis in the GRP94 chaperone cycle.
+The line below this paragraph, {{ABSTRACT_PUBMED_17936703}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17936703 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17936703}}
 ==About this Structure==
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 [[Category: Hsp90]]
 [[Category: Htpg]]
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