2o1v
From Proteopedia
(New page: 200px<br /><applet load="2o1v" size="350" color="white" frame="true" align="right" spinBox="true" caption="2o1v, resolution 2.45Å" /> '''Structure of full le...) |
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==Overview== | ==Overview== | ||
| - | GRP94, an essential endoplasmic reticulum chaperone, is required for the | + | 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== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Structures of GRP94- | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17936703 17936703] |
[[Category: Canis lupus familiaris]] | [[Category: Canis lupus familiaris]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dollins, D | + | [[Category: Dollins, D E.]] |
| - | [[Category: Gewirth, D | + | [[Category: Gewirth, D T.]] |
| - | [[Category: Immormino, R | + | [[Category: Immormino, R M.]] |
| - | [[Category: Warren, J | + | [[Category: Warren, J J.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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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 Thu Feb 21 18:13:39 2008'' |
Revision as of 16:13, 21 February 2008
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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 with and as ligands. 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 Thu Feb 21 18:13:39 2008
Categories: Canis lupus familiaris | Single protein | Dollins, D E. | Gewirth, D T. | Immormino, R M. | Warren, J J. | ADP | MG | Adp | Chaperone | Endoplasmin | Gp96 | Grp94 | Hsp82 | Hsp90 | Htpg
