2weq: Difference between revisions

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-{{Seed}}
-[[Image:2weq.png|left|200px]]
-<!--
+==Yeast Hsp90 N-terminal domain LI-IV mutant with Geldanamycin==
-The line below this paragraph, containing "STRUCTURE_2weq", creates the "Structure Box" on the page.
+<StructureSection load='2weq' size='340' side='right'caption='[[2weq]], [[Resolution|resolution]] 2.20&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'>[[2weq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WEQ 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]] 2.2&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDM:GELDANAMYCIN'>GDM</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-{{STRUCTURE_2weq|  PDB=2weq  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2weq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2weq OCA], [https://pdbe.org/2weq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2weq RCSB], [https://www.ebi.ac.uk/pdbsum/2weq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2weq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HSP82_YEAST HSP82_YEAST] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.<ref>PMID:17114002</ref>
+== 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/we/2weq_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=2weq ConSurf].
+<div style="clear:both"></div>
-===YEAST HSP90 N-TERMINAL DOMAIN LI-IV MUTANT WITH GELDANAMYCIN===
+==See Also==
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
+== References ==
-<!--
+<references/>
-The line below this paragraph, {{ABSTRACT_PUBMED_19236053}}, adds the Publication Abstract to the page
+__TOC__
-(as it appears on PubMed at http://www.pubmed.gov), where 19236053 is the PubMed ID number.
+</StructureSection>
--->
+[[Category: Large Structures]]
-{{ABSTRACT_PUBMED_19236053}}
-==About this Structure==
-WEQ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WEQ OCA].
-==Reference==
-<ref group="xtra">PMID:19236053</ref><references group="xtra"/>
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Pearl, L H.]]
+[[Category: Pearl LH]]
-[[Category: Prodromou, C.]]
+[[Category: Prodromou C]]
-[[Category: Roe, S M.]]
+[[Category: Roe SM]]
-[[Category: Atp-binding]]
-[[Category: Atpase]]
-[[Category: Chaperone]]
-[[Category: Cytoplasm]]
-[[Category: Nucleotide-binding]]
-[[Category: Phosphoprotein]]
-[[Category: Stress response]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May  6 09:58:09 2009''