3P2M

Crystal Structure of a Novel Esterase Rv0045c from Mycobacterium tuberculosis

3P2M の概要

• エントリーDOI: 10.2210/pdb3p2m/pdb
• 分子名称: POSSIBLE HYDROLASE (2 entities in total)
• 機能のキーワード: alpha/beta hydrolase superfamily, hydrolase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35544.79

構造登録者

Zheng, X.D.,Guo, J.,Xu, L.,Li, H.,Zhang, D.,Zhang, K.,Sun, F.,Wen, T.,Liu, S.,Pang, H. (登録日: 2010-10-03, 公開日: 2011-07-06, 最終更新日: 2024-03-20)

主引用文献

Zheng, X.D.,Guo, J.,Xu, L.,Li, H.,Zhang, D.,Zhang, K.,Sun, F.,Wen, T.,Liu, S.,Pang, H.
Crystal Structure of a Novel Esterase Rv0045c from Mycobacterium tuberculosis
Plos One, 6:e20506-e20506, 2011

PubMed Abstract: There are at least 250 enzymes in Mycobacterium tuberculosis (M. tuberculosis) involved in lipid metabolism. Some of the enzymes are required for bacterial survival and full virulence. The esterase Rv0045c shares little amino acid sequence similarity with other members of the esterase/lipase family. Here, we report the 3D structure of Rv0045c. Our studies demonstrated that Rv0045c is a novel member of α/β hydrolase fold family. The structure of esterase Rv0045c contains two distinct domains: the α/β fold domain and the cap domain. The active site of esterase Rv0045c is highly conserved and comprised of two residues: Ser154 and His309. We proposed that Rv0045c probably employs two kinds of enzymatic mechanisms when hydrolyzing C-O ester bonds within substrates. The structure provides insight into the hydrolysis mechanism of the C-O ester bond, and will be helpful in understanding the ester/lipid metabolism in M. tuberculosis.

PubMed: 21637775
DOI: 10.1371/journal.pone.0020506

実験手法

X-RAY DIFFRACTION (2.8 Å)