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==Crystal structure of Thermotoga maritima CheB methylesterase catalytic domain== | |||
=== | <StructureSection load='3sft' size='340' side='right' caption='[[3sft]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3sft]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SFT FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cheB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-glutamate_methylesterase Protein-glutamate methylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.61 3.1.1.61] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sft OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sft RCSB], [http://www.ebi.ac.uk/pdbsum/3sft PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We 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<ref>PMID:21722627</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== | ==See Also== | ||
*[[Methylesterase|Methylesterase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Protein-glutamate methylesterase]] | [[Category: Protein-glutamate methylesterase]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
[[Category: Crane, B R | [[Category: Crane, B R]] | ||
[[Category: Park, S Y | [[Category: Park, S Y]] | ||
[[Category: Chemoreceptor]] | [[Category: Chemoreceptor]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Methylesterase]] | [[Category: Methylesterase]] | ||
[[Category: Modified doubly-wound/fold]] | [[Category: Modified doubly-wound/fold]] | ||
Revision as of 10:16, 21 December 2014
Crystal structure of Thermotoga maritima CheB methylesterase catalytic domainCrystal structure of Thermotoga maritima CheB methylesterase catalytic domain
Structural highlights
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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