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| {{STRUCTURE_2o1w| PDB=2o1w | SCENE= }} | | {{STRUCTURE_2o1w| PDB=2o1w | SCENE= }} |
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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=== |
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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.
| | 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}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hsp90]] | | [[Category: Hsp90]] |
| [[Category: Htpg]] | | [[Category: Htpg]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:12:36 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:19:50 2008'' |