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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/Atcc_43589 Atcc 43589]. 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> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cheB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr> | + | </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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-glutamate_methylesterase Protein-glutamate methylesterase], with EC number [https://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'>[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).
| + | [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: Atcc 43589]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Protein-glutamate methylesterase]] | + | [[Category: Thermotoga maritima]] |
| - | [[Category: Crane, B R]] | + | [[Category: Crane BR]] |
| - | [[Category: Park, S Y]] | + | [[Category: Park SY]] |
| - | [[Category: Chemoreceptor]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Methylesterase]]
| + | |
| - | [[Category: Modified doubly-wound/fold]]
| + | |
| Structural highlights
Function
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).
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cho KH, Crane BR, Park S. An insight into the interaction mode between CheB and chemoreceptor from two crystal structures of CheB methylesterase catalytic domain. 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 doi:10.1016/j.bbrc.2011.06.090
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