3sft: Difference between revisions
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<StructureSection load='3sft' size='340' side='right'caption='[[3sft]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='3sft' size='340' side='right'caption='[[3sft]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3sft]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3sft]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SFT 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]] 2.15Å</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=3sft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sft OCA], [https://pdbe.org/3sft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sft RCSB], [https://www.ebi.ac.uk/pdbsum/3sft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sft 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=3sft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sft OCA], [https://pdbe.org/3sft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sft RCSB], [https://www.ebi.ac.uk/pdbsum/3sft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sft ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CHEB_THEMA CHEB_THEMA] Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR (By similarity). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermotoga maritima]] | ||
[[Category: Crane | [[Category: Crane BR]] | ||
[[Category: Park | [[Category: Park SY]] | ||
Latest revision as of 20:25, 1 November 2023
Crystal structure of Thermotoga maritima CheB methylesterase catalytic domainCrystal structure of Thermotoga maritima CheB methylesterase catalytic domain
Structural highlights
FunctionCHEB_THEMA Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR (By similarity). Publication Abstract from PubMedWe have determined 2.2 A resolution crystal structure of Thermotoga maritima CheB methylesterase domain to provide insight into the interaction mode between CheB and chemoreceptors. T. maritima CheB methylesterase domain has identical topology of a modified doubly-wound alpha/beta fold that was observed from the previously reported Salmonella typhimurium counterpart, but the analysis of the electrostatic potential surface near the catalytic triad indicated considerable charge distribution difference. As the CheB demethylation consensus sites of the chemoreceptors, the CheB substrate, are not uniquely conserved between T. maritima and S. typhimurium, such surfaces with differing electrostatic properties may reflect CheB regions that mediate protein-protein interaction. Via the computational docking of the two T. maritima and S. typhimurium CheB structures to the respective T. maritima and Escherichia coli chemoreceptors, we propose a CheB:chemoreceptor interaction mode. An insight into the interaction mode between CheB and chemoreceptor from two crystal structures of CheB methylesterase catalytic domain.,Cho KH, Crane BR, Park S Biochem Biophys Res Commun. 2011 Jul 22;411(1):69-75. doi:, 10.1016/j.bbrc.2011.06.090. Epub 2011 Jun 21. PMID:21722627[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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