3SFT

Crystal structure of Thermotoga maritima CheB methylesterase catalytic domain

Summary for 3SFT

• Entry DOI: 10.2210/pdb3sft/pdb
• Descriptor: Chemotaxis response regulator protein-glutamate methylesterase (2 entities in total)
• Functional Keywords: modified doubly-wound/fold, methylesterase, chemoreceptor, hydrolase
• Biological source: Thermotoga maritima
• Cellular location: Cytoplasm (By similarity): Q9WYN9
• Total number of polymer chains: 1
• Total formula weight: 20895.29

Authors

Park, S.Y.,Crane, B.R. (deposition date: 2011-06-14, release date: 2011-07-20, Last modification date: 2023-11-01)

Primary citation

Cho, K.H.,Crane, B.R.,Park, S.Y.
An insight into the interaction mode between CheB and chemoreceptor from two crystal structures of CheB methylesterase catalytic domain
Biochem.Biophys.Res.Commun., 411:69-75, 2011

PubMed 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.

PubMed: 21722627
DOI: 10.1016/j.bbrc.2011.06.090

Experimental method

X-RAY DIFFRACTION (2.15 Å)