2o1v

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[[Image:2o1v.jpg|left|200px]]
 
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{{Structure
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==Structure of full length GRP94 with ADP bound==
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|PDB= 2o1v |SIZE=350|CAPTION= <scene name='initialview01'>2o1v</scene>, resolution 2.45&Aring;
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<StructureSection load='2o1v' size='340' side='right'caption='[[2o1v]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>
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<table><tr><td colspan='2'>[[2o1v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. The December 2008 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Hsp90'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2008_12 10.2210/rcsb_pdb/mom_2008_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O1V FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
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|GENE= HSP90B1, TRA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 Canis lupus familiaris])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o1v OCA], [https://pdbe.org/2o1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o1v RCSB], [https://www.ebi.ac.uk/pdbsum/2o1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o1v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o1/2o1v_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2o1v ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Structure of full length GRP94 with ADP bound'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2o1v" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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== References ==
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==About this Structure==
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<references/>
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2O1V 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=2O1V OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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]
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[[Category: Canis lupus familiaris]]
[[Category: Canis lupus familiaris]]
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[[Category: Single protein]]
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[[Category: Hsp90]]
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[[Category: Dollins, D E.]]
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[[Category: Large Structures]]
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[[Category: Gewirth, D T.]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Immormino, R M.]]
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[[Category: Dollins DE]]
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[[Category: Warren, J J.]]
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[[Category: Gewirth DT]]
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[[Category: ADP]]
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[[Category: Immormino RM]]
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[[Category: MG]]
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[[Category: Warren JJ]]
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[[Category: adp]]
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[[Category: chaperone]]
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[[Category: endoplasmin]]
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[[Category: gp96]]
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[[Category: grp94]]
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[[Category: hsp82]]
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[[Category: hsp90]]
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[[Category: htpg]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:54:01 2008''
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Current revision

Structure of full length GRP94 with ADP bound

PDB ID 2o1v

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