2o1v

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{{STRUCTURE_2o1v| PDB=2o1v | SCENE= }}
{{STRUCTURE_2o1v| PDB=2o1v | SCENE= }}
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'''Structure of full length GRP94 with ADP bound'''
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===Structure of full length GRP94 with ADP bound===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_17936703}}, adds the Publication Abstract to the page
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(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==
==About this Structure==
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[[Category: Hsp90]]
[[Category: Hsp90]]
[[Category: Htpg]]
[[Category: Htpg]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:12:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:11:37 2008''

Revision as of 00:11, 29 July 2008

Image:2o1v.png

Template:STRUCTURE 2o1v

Structure of full length GRP94 with ADP bound

Template:ABSTRACT PUBMED 17936703

About this Structure

2O1V is a Single protein structure of sequence from Canis lupus familiaris. Full crystallographic information is available from OCA.

Reference

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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