2o1w: Difference between revisions
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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]], [[2o1t|2O1T]], [[1yt1|1YT1]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o1w OCA], [http://www.ebi.ac.uk/pdbsum/2o1w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2o1w RCSB]</span> | |||
}} | }} | ||
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[[Category: Warren, J J.]] | [[Category: Warren, J J.]] | ||
[[Category: chaperone]] | [[Category: chaperone]] | ||
[[Category: endoplasmin]] | [[Category: endoplasmin,]] | ||
[[Category: gp96]] | [[Category: gp96]] | ||
[[Category: grp94]] | [[Category: grp94]] | ||
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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 04:11:33 2008'' | ||
Revision as of 04:11, 31 March 2008
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| , resolution 3.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | HSP90B1, TRA1 (Canis lupus familiaris) | ||||||
| Related: | 2O1U, 2O1V, 2O1T, 1YT1
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of N-terminal plus middle domains (N+M) of GRP94
OverviewOverview
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 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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