1tc6: Difference between revisions

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-[[Image:1tc6.gif|left|200px]]<br /><applet load="1tc6" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1tc6, resolution 1.87&Aring;" />
-'''Ligand Induced Conformational Shift in the N-terminal Domain of GRP94, Open Conformation ADP-Complex'''<br />
-==Overview==
+==Ligand Induced Conformational Shift in the N-terminal Domain of GRP94, Open Conformation ADP-Complex==
-GRP94 is the endoplasmic reticulum paralog of cytoplasmic Hsp90. Models of Hsp90 action posit an ATP-dependent conformational switch in the N-terminal ligand regulatory domain of the chaperone. However, crystal structures of the isolated N-domain of Hsp90 in complex with a variety of ligands have yet to demonstrate such a conformational change. We have determined the structure of the N-domain of GRP94 in complex with ATP, ADP, and AMP. Compared with the N-ethylcarboxamidoadenosine and radicicol-bound forms, these structures reveal a large conformational rearrangement in the protein. The nucleotide-bound form exposes new surfaces that interact to form a biochemically plausible dimer that is reminiscent of those seen in structures of MutL and DNA gyrase. Weak ATP binding and a conformational change in response to ligand identity are distinctive mechanistic features of GRP94 and suggest a model for how GRP94 functions in the absence of co-chaperones and ATP hydrolysis.
+<StructureSection load='1tc6' size='340' side='right'caption='[[1tc6]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1tc6]] is a 2 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=1TC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TC6 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87&#8491;</td></tr>
+<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>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></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=1tc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tc6 OCA], [https://pdbe.org/1tc6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tc6 RCSB], [https://www.ebi.ac.uk/pdbsum/1tc6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tc6 ProSAT]</span></td></tr>
+</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/tc/1tc6_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=1tc6 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-TC6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=PG4:'>PG4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TC6 OCA].
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone., Immormino RM, Dollins DE, Shaffer PL, Soldano KL, Walker MA, Gewirth DT, J Biol Chem. 2004 Oct 29;279(44):46162-71. Epub 2004 Aug 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15292259 15292259]
 [[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: Shaffer, P L.]]
+[[Category: Shaffer PL]]
-[[Category: Soldano, K L.]]
+[[Category: Soldano KL]]
-[[Category: Walker, M A.]]
+[[Category: Walker MA]]
-[[Category: ADP]]
-[[Category: MG]]
-[[Category: PG4]]
-[[Category: adp]]
-[[Category: bergerat]]
-[[Category: chaperone]]
-[[Category: endoplasmic reticulum]]
-[[Category: grp94]]
-[[Category: hsp90]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:06 2008''