2gq0: Difference between revisions

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-{{Seed}}
-[[Image:2gq0.png|left|200px]]
-<!--
+==Crystal Structure of the Middle Domain of HtpG, the E. coli Hsp90==
-The line below this paragraph, containing "STRUCTURE_2gq0", creates the "Structure Box" on the page.
+<StructureSection load='2gq0' size='340' side='right'caption='[[2gq0]], [[Resolution|resolution]] 1.90&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'>[[2gq0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GQ0 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]] 1.9&#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=2gq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gq0 OCA], [https://pdbe.org/2gq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gq0 RCSB], [https://www.ebi.ac.uk/pdbsum/2gq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gq0 ProSAT]</span></td></tr>
-{{STRUCTURE_2gq0|  PDB=2gq0  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HTPG_ECOLI HTPG_ECOLI] Molecular chaperone. Has ATPase activity.[HAMAP-Rule:MF_00505]
+== 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/gq/2gq0_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=2gq0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+In eukaryotes, the ubiquitous and abundant members of the 90 kilodalton heat-shock protein (hsp90) chaperone family facilitate the folding and conformational changes of a broad array of proteins important in cell signaling, proliferation, and survival. Here we describe the effects of nucleotides on the structure of full-length HtpG, the Escherichia coli hsp90 ortholog. By electron microscopy, the nucleotide-free, AMPPNP bound, and ADP bound states of HtpG adopt completely distinct conformations. Structural characterization of nucleotide-free and ADP bound HtpG was extended to higher resolution by X-ray crystallography. In the absence of nucleotide, HtpG exhibits an "open" conformation in which the three domains of each monomer present hydrophobic elements into the large cleft formed by the dimer. By contrast, ADP binding drives dramatic conformational changes that allow these hydrophobic elements to converge and shield each other from solvent, suggesting a mechanism by which nucleotides could control client protein binding and release.
-===Crystal Structure of the Middle Domain of HtpG, the E. coli Hsp90===
+Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements.,Shiau AK, Harris SF, Southworth DR, Agard DA Cell. 2006 Oct 20;127(2):329-40. PMID:17055434<ref>PMID:17055434</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2gq0" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17055434}}, 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 17055434 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17055434}}
+__TOC__
+</StructureSection>
-==About this Structure==
-GQ0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GQ0 OCA].
-==Reference==
-Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements., Shiau AK, Harris SF, Southworth DR, Agard DA, Cell. 2006 Oct 20;127(2):329-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17055434 17055434]
 [[Category: Escherichia coli]]
-[[Category: Non-chaperonin molecular chaperone ATPase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Agard DA]]
-[[Category: Agard, D A.]]
+[[Category: Harris SF]]
-[[Category: Harris, S F.]]
+[[Category: Shiau AK]]
-[[Category: Shiau, A K.]]
-[[Category: E. coli]]
-[[Category: Hsp90]]
-[[Category: Htpg]]
-[[Category: Molecular chaperone]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:39:44 2008''