2o1t
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= HSP90B1, TRA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 Canis lupus familiaris]) | |GENE= HSP90B1, TRA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 Canis lupus familiaris]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2o1u|2O1U]], [[2o1v|2O1V]], [[2o1w|2O1W]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o1t OCA], [http://www.ebi.ac.uk/pdbsum/2o1t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2o1t RCSB]</span> | ||
}} | }} | ||
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[[Category: htpg]] | [[Category: htpg]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:11:30 2008'' |
Revision as of 01:11, 31 March 2008
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| , resolution 3.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | HSP90B1, TRA1 (Canis lupus familiaris) | ||||||
| Related: | 2O1U, 2O1V, 2O1W
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of Middle plus C-terminal domains (M+C) 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.
About this Structure
2O1T 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 Mon Mar 31 04:11:30 2008
Categories: Canis lupus familiaris | Single protein | Dollins, D E. | Gewirth, D T. | Immormino, R M. | Warren, J J. | Chaperone | Endoplasmin | Gp96 | Grp94 | Hsp82 | Hsp90 | Htpg
