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
