2o1w: Difference between revisions

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-{{Seed}}
-[[Image:2o1w.png|left|200px]]
-<!--
+==Structure of N-terminal plus middle domains (N+M) of GRP94==
-The line below this paragraph, containing "STRUCTURE_2o1w", creates the "Structure Box" on the page.
+<StructureSection load='2o1w' size='340' side='right'caption='[[2o1w]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4&#8491;</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>
-{{STRUCTURE_2o1w|  PDB=2o1w  |  SCENE=  }}
+</table>
+== Function ==
+[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/o1/2o1w_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=2o1w 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 N-terminal plus middle domains (N+M) 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 2o1w" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17936703}}, adds the Publication Abstract to the page
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17936703 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17936703}}
+__TOC__
+</StructureSection>
-==About this Structure==
-O1W is a 5 chains structure of sequences 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=2O1W OCA].
-==Reference==
-<ref group="xtra">PMID:17936703</ref><references group="xtra"/>
 [[Category: Canis lupus familiaris]]
-[[Category: Dollins, D E.]]
+[[Category: Large Structures]]
-[[Category: Gewirth, D T.]]
+[[Category: Dollins DE]]
-[[Category: Immormino, R M.]]
+[[Category: Gewirth DT]]
-[[Category: Warren, J J.]]
+[[Category: Immormino RM]]
-[[Category: Chaperone]]
+[[Category: Warren JJ]]
-[[Category: Endoplasmin]]
-[[Category: Gp96]]
-[[Category: Grp94]]
-[[Category: Hsp82]]
-[[Category: Hsp90]]
-[[Category: Htpg]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 14:38:22 2009''