2o1v
From Proteopedia
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[[Image:2o1v.jpg|left|200px]] | [[Image:2o1v.jpg|left|200px]] | ||
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'''Structure of full length GRP94 with ADP bound''' | '''Structure of full length GRP94 with ADP bound''' | ||
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[[Category: Immormino, R M.]] | [[Category: Immormino, R M.]] | ||
[[Category: Warren, J J.]] | [[Category: Warren, J J.]] | ||
- | [[Category: | + | [[Category: Adp]] |
- | [[Category: | + | [[Category: Chaperone]] |
- | [[Category: | + | [[Category: Endoplasmin]] |
- | [[Category: | + | [[Category: Gp96]] |
- | [[Category: | + | [[Category: Grp94]] |
- | [[Category: | + | [[Category: Hsp82]] |
- | [[Category: | + | [[Category: Hsp90]] |
- | [[Category: | + | [[Category: Htpg]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:12:33 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 07:12, 4 May 2008
Structure of full length GRP94 with ADP bound
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.
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 Page seeded by OCA on Sun May 4 10:12:33 2008
Categories: Canis lupus familiaris | Single protein | Dollins, D E. | Gewirth, D T. | Immormino, R M. | Warren, J J. | Adp | Chaperone | Endoplasmin | Gp96 | Grp94 | Hsp82 | Hsp90 | Htpg