3P2M

Crystal Structure of a Novel Esterase Rv0045c from Mycobacterium tuberculosis

Summary for 3P2M

• Entry DOI: 10.2210/pdb3p2m/pdb
• Descriptor: POSSIBLE HYDROLASE (2 entities in total)
• Functional Keywords: alpha/beta hydrolase superfamily, hydrolase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 35544.79

Authors

Zheng, X.D.,Guo, J.,Xu, L.,Li, H.,Zhang, D.,Zhang, K.,Sun, F.,Wen, T.,Liu, S.,Pang, H. (deposition date: 2010-10-03, release date: 2011-07-06, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)