2gq0: Difference between revisions
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<StructureSection load='2gq0' size='340' side='right'caption='[[2gq0]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='2gq0' size='340' side='right'caption='[[2gq0]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2gq0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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> | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/HTPG_ECOLI HTPG_ECOLI] Molecular chaperone. Has ATPase activity.[HAMAP-Rule:MF_00505] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Agard DA]] | |||
[[Category: Agard | [[Category: Harris SF]] | ||
[[Category: Harris | [[Category: Shiau AK]] | ||
[[Category: Shiau | |||
Latest revision as of 12:46, 30 August 2023
Crystal Structure of the Middle Domain of HtpG, the E. coli Hsp90Crystal Structure of the Middle Domain of HtpG, the E. coli Hsp90
Structural highlights
FunctionHTPG_ECOLI Molecular chaperone. Has ATPase activity.[HAMAP-Rule:MF_00505] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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