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| | <StructureSection load='2o1w' size='340' side='right'caption='[[2o1w]], [[Resolution|resolution]] 3.40Å' scene=''> | | <StructureSection load='2o1w' size='340' side='right'caption='[[2o1w]], [[Resolution|resolution]] 3.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2o1w]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Canfa Canfa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O1W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O1W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2o1w]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O1W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O1W FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2o1u|2o1u]], [[2o1v|2o1v]], [[2o1t|2o1t]], [[1yt1|1yt1]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90B1, TRA1 ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2o1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o1w OCA], [https://pdbe.org/2o1w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o1w RCSB], [https://www.ebi.ac.uk/pdbsum/2o1w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o1w ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o1w OCA], [https://pdbe.org/2o1w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o1w RCSB], [https://www.ebi.ac.uk/pdbsum/2o1w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o1w ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ENPL_CANFA 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).
| + | [https://www.uniprot.org/uniprot/ENPL_CANLF ENPL_CANLF] 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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Canfa]] | + | [[Category: Canis lupus familiaris]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dollins, D E]] | + | [[Category: Dollins DE]] |
| - | [[Category: Gewirth, D T]] | + | [[Category: Gewirth DT]] |
| - | [[Category: Immormino, R M]] | + | [[Category: Immormino RM]] |
| - | [[Category: Warren, J J]] | + | [[Category: Warren JJ]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Endoplasmin]]
| + | |
| - | [[Category: Gp96]]
| + | |
| - | [[Category: Grp94]]
| + | |
| - | [[Category: Hsp82]]
| + | |
| - | [[Category: Hsp90]]
| + | |
| - | [[Category: Htpg]]
| + | |
| Structural highlights
Function
ENPL_CANLF 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 PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dollins DE, Warren JJ, Immormino RM, Gewirth DT. Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones. Mol Cell. 2007 Oct 12;28(1):41-56. PMID:17936703 doi:10.1016/j.molcel.2007.08.024
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