title: An insight into the interaction mode between CheB and chemoreceptor from two crystal structures of CheB methylesterase catalytic domain.
abstract: We have determined 2.2 Å 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 α/β 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.
authors: School of Systems Biomedical Science, Soongsil University, Seoul, Republic of Korea.
authors: Kwang-Hwi
authors: KH
authors: Cho
authors: Brian R
authors: BR
authors: Crane
authors: Sangyoun
authors: S
authors: Park
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000235:genetics; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012486:Salmonella typhimurium / Q000201:enzymology; D020124:Thermotoga maritima / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; C069656:CheB protein, Bacteria; D002265:Carboxylic Ester Hydrolases; C041144:chemotactic protein methylesterase