1u2o: Difference between revisions

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-[[Image:1u2o.jpg|left|200px]]
- {{Structure
+==Crystal Structure Of The N-Domain Of Grp94 Lacking The Charged Domain In Complex With Neca==
-|PDB= 1u2o |SIZE=350|CAPTION= <scene name='initialview01'>1u2o</scene>, resolution 2.10&Aring;
+<StructureSection load='1u2o' size='340' side='right'caption='[[1u2o]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=NEC:N-ETHYL-5&#39;-CARBOXAMIDO+ADENOSINE'>NEC</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>
+<table><tr><td colspan='2'>[[1u2o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1qyh 1qyh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U2O 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]] 2.1&#8491;</td></tr>
-|GENE= TRA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 Canis lupus familiaris])
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=NEC:N-ETHYL-5-CARBOXAMIDO+ADENOSINE'>NEC</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1u2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2o OCA], [https://pdbe.org/1u2o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u2o RCSB], [https://www.ebi.ac.uk/pdbsum/1u2o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u2o ProSAT]</span></td></tr>
-|RELATEDENTRY=[[1qy5|1QY5]], [[1qy8|1QY8]], [[1qye|1QYE]]
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2o OCA], [http://www.ebi.ac.uk/pdbsum/1u2o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u2o RCSB]</span>
+== 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/u2/1u2o_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=1u2o ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+GRP94, the endoplasmic reticulum (ER) paralog of the chaperone Hsp90, plays an essential role in the structural maturation or secretion of a subset of proteins destined for transport to the cell surface, such as the Toll-like receptors 2 and 4, and IgG, respectively. GRP94 differs from cytoplasmic Hsp90 by exhibiting very weak ATP binding and hydrolysis activity. GRP94 also binds selectively to a series of substituted adenosine analogs. The high resolution crystal structures at 1.75-2.1 A of the N-terminal and adjacent charged domains of GRP94 in complex with N-ethylcarboxamidoadenosine, radicicol, and 2-chlorodideoxyadenosine reveals a structural mechanism for ligand discrimination among hsp90 family members. The structures also identify a putative subdomain that may act as a ligand-responsive switch. The residues of the charged region fold into a disordered loop whose termini are ordered and continue the twisted beta sheet that forms the structural core of the N-domain. This continuation of the beta sheet past the charged domain suggests a structural basis for the association of the N-terminal and middle domains of the full-length chaperone.
-'''Crystal Structure Of The N-Domain Of Grp94 Lacking The Charged Domain In Complex With Neca'''
+Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation.,Soldano KL, Jivan A, Nicchitta CV, Gewirth DT J Biol Chem. 2003 Nov 28;278(48):48330-8. Epub 2003 Sep 11. PMID:12970348<ref>PMID:12970348</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1u2o" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-GRP94, the endoplasmic reticulum (ER) paralog of the chaperone Hsp90, plays an essential role in the structural maturation or secretion of a subset of proteins destined for transport to the cell surface, such as the Toll-like receptors 2 and 4, and IgG, respectively. GRP94 differs from cytoplasmic Hsp90 by exhibiting very weak ATP binding and hydrolysis activity. GRP94 also binds selectively to a series of substituted adenosine analogs. The high resolution crystal structures at 1.75-2.1 A of the N-terminal and adjacent charged domains of GRP94 in complex with N-ethylcarboxamidoadenosine, radicicol, and 2-chlorodideoxyadenosine reveals a structural mechanism for ligand discrimination among hsp90 family members. The structures also identify a putative subdomain that may act as a ligand-responsive switch. The residues of the charged region fold into a disordered loop whose termini are ordered and continue the twisted beta sheet that forms the structural core of the N-domain. This continuation of the beta sheet past the charged domain suggests a structural basis for the association of the N-terminal and middle domains of the full-length chaperone.
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
+== References ==
-==About this Structure==
+<references/>
-U2O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. This structure supersedes the now removed PDB entry 1QYH. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2O OCA].
+__TOC__
+</StructureSection>
-==Reference==
-Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation., Soldano KL, Jivan A, Nicchitta CV, Gewirth DT, J Biol Chem. 2003 Nov 28;278(48):48330-8. Epub 2003 Sep 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12970348 12970348]
 [[Category: Canis lupus familiaris]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Gewirth, D T.]]
+[[Category: Gewirth DT]]
-[[Category: Jivan, A.]]
+[[Category: Jivan A]]
-[[Category: Nicchitta, C V.]]
+[[Category: Nicchitta CV]]
-[[Category: Soldano, K L.]]
+[[Category: Soldano KL]]
-[[Category: bergerat]]
-[[Category: chaperone]]
-[[Category: endoplasmic reticulum]]
-[[Category: grp94]]
-[[Category: hsp90]]
-[[Category: neca]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:04:34 2008''