2o1t: Difference between revisions

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-[[Image:2o1t.jpg|left|200px]]
- {{Structure
+==Structure of Middle plus C-terminal domains (M+C) of GRP94==
-|PDB= 2o1t |SIZE=350|CAPTION= <scene name='initialview01'>2o1t</scene>, resolution 3.20&Aring;
+<StructureSection load='2o1t' size='340' side='right'caption='[[2o1t]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[2o1t]] is a 10 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=2O1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O1T FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
-|GENE= HSP90B1, TRA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 Canis lupus familiaris])
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o1t OCA], [https://pdbe.org/2o1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o1t RCSB], [https://www.ebi.ac.uk/pdbsum/2o1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o1t ProSAT]</span></td></tr>
-|DOMAIN=
+</table>
-|RELATEDENTRY=[[2o1u|2O1U]], [[2o1v|2O1V]], [[2o1w|2O1W]]
+== Function ==
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o1t OCA], [http://www.ebi.ac.uk/pdbsum/2o1t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2o1t RCSB]</span>
+[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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o1/2o1t_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2o1t ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-'''Structure of Middle plus C-terminal domains (M+C) 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:17936703<ref>PMID:17936703</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2o1t" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
+== References ==
-==About this Structure==
+<references/>
-O1T is a [[Single protein]] structure of sequence from [http://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=2O1T OCA].
+__TOC__
+</StructureSection>
-==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:[http://www.ncbi.nlm.nih.gov/pubmed/17936703 17936703]
 [[Category: Canis lupus familiaris]]
-[[Category: Single protein]]
+[[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]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:11:30 2008''