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2o1u

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[[Image:2o1u.jpg|left|200px]]
[[Image:2o1u.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2o1u |SIZE=350|CAPTION= <scene name='initialview01'>2o1u</scene>, resolution 2.40&Aring;
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The line below this paragraph, containing "STRUCTURE_2o1u", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE= HSP90B1, TRA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 Canis lupus familiaris])
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-->
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|DOMAIN=
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{{STRUCTURE_2o1u| PDB=2o1u | SCENE= }}
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|RELATEDENTRY=[[2o1v|2O1V]], [[2o1w|2O1W]], [[2o1t|2O1T]], [[1tc6|1TC6]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o1u OCA], [http://www.ebi.ac.uk/pdbsum/2o1u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2o1u RCSB]</span>
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}}
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'''Structure of full length GRP94 with AMP-PNP bound'''
'''Structure of full length GRP94 with AMP-PNP bound'''
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[[Category: Immormino, R M.]]
[[Category: Immormino, R M.]]
[[Category: Warren, J J.]]
[[Category: Warren, J J.]]
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[[Category: amp-pnp]]
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[[Category: Amp-pnp]]
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[[Category: chaperone]]
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[[Category: Chaperone]]
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[[Category: endoplasmin,]]
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[[Category: Endoplasmin]]
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[[Category: gp96]]
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[[Category: Gp96]]
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[[Category: grp94]]
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[[Category: Grp94]]
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[[Category: hsp82]]
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[[Category: Hsp82]]
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[[Category: hsp90]]
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[[Category: Hsp90]]
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[[Category: htpg]]
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[[Category: Htpg]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:12:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:11:29 2008''
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Revision as of 07:12, 4 May 2008

Image:2o1u.jpg

Template:STRUCTURE 2o1u

Structure of full length GRP94 with AMP-PNP 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

2O1U 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 10:12:23 2008

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