3SFT

Crystal structure of Thermotoga maritima CheB methylesterase catalytic domain

3SFT の概要

• エントリーDOI: 10.2210/pdb3sft/pdb
• 分子名称: Chemotaxis response regulator protein-glutamate methylesterase (2 entities in total)
• 機能のキーワード: modified doubly-wound/fold, methylesterase, chemoreceptor, hydrolase
• 由来する生物種: Thermotoga maritima
• 細胞内の位置: Cytoplasm (By similarity): Q9WYN9
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20895.29

構造登録者

Park, S.Y.,Crane, B.R. (登録日: 2011-06-14, 公開日: 2011-07-20, 最終更新日: 2023-11-01)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.15 Å)