1tc0: Difference between revisions
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==Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP== | ==Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP== | ||
<StructureSection load='1tc0' size='340' side='right' caption='[[1tc0]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1tc0' size='340' side='right' caption='[[1tc0]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qy5|1qy5]], [[1qy8|1qy8]], [[1qye|1qye]], [[1qyh|1qyh]], [[1tbw|1tbw]], [[1tc6|1tc6]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qy5|1qy5]], [[1qy8|1qy8]], [[1qye|1qye]], [[1qyh|1qyh]], [[1tbw|1tbw]], [[1tc6|1tc6]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 CANFA])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 CANFA])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tc0 OCA], [http://pdbe.org/1tc0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tc0 RCSB], [http://www.ebi.ac.uk/pdbsum/1tc0 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tc0 OCA], [http://pdbe.org/1tc0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tc0 RCSB], [http://www.ebi.ac.uk/pdbsum/1tc0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tc0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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[[Category: Soldano, K L]] | [[Category: Soldano, K L]] | ||
[[Category: Walker, M A]] | [[Category: Walker, M A]] | ||
[[Category: Atp]] | |||
[[Category: Bergerat]] | [[Category: Bergerat]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
Revision as of 14:17, 7 October 2017
Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATPLigand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP
Structural highlights
Function[ENPL_CANFA] Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGRP94 is the endoplasmic reticulum paralog of cytoplasmic Hsp90. Models of Hsp90 action posit an ATP-dependent conformational switch in the N-terminal ligand regulatory domain of the chaperone. However, crystal structures of the isolated N-domain of Hsp90 in complex with a variety of ligands have yet to demonstrate such a conformational change. We have determined the structure of the N-domain of GRP94 in complex with ATP, ADP, and AMP. Compared with the N-ethylcarboxamidoadenosine and radicicol-bound forms, these structures reveal a large conformational rearrangement in the protein. The nucleotide-bound form exposes new surfaces that interact to form a biochemically plausible dimer that is reminiscent of those seen in structures of MutL and DNA gyrase. Weak ATP binding and a conformational change in response to ligand identity are distinctive mechanistic features of GRP94 and suggest a model for how GRP94 functions in the absence of co-chaperones and ATP hydrolysis. Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone.,Immormino RM, Dollins DE, Shaffer PL, Soldano KL, Walker MA, Gewirth DT J Biol Chem. 2004 Oct 29;279(44):46162-71. Epub 2004 Aug 2. PMID:15292259[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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