2VF2

X-ray crystal structure of HsaD from Mycobacterium tuberculosis

2VF2 の概要

• エントリーDOI: 10.2210/pdb2vf2/pdb
• 分子名称: 2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOATE HYDROLASE BPHD, GLYCEROL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: meta-cleavage product hydrolase, hsad, hydrolase, serine hydrolase
• 由来する生物種: MYCOBACTERIUM TUBERCULOSIS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68641.90

構造登録者

Lack, N.,Lowe, E.D.,Liu, J.,Eltis, L.D.,Noble, M.E.M.,Sim, E.,Westwood, I.M. (登録日: 2007-10-29, 公開日: 2007-11-06, 最終更新日: 2023-12-13)

主引用文献

Lack, N.,Lowe, E.D.,Liu, J.,Eltis, L.D.,Noble, M.E.M.,Sim, E.,Westwood, I.M.
Structure of Hsad, a Steroid-Degrading Hydrolase, from Mycobacterium Tuberculosis.
Acta Crystallogr.,Sect.F, 64:2-, 2008

PubMed Abstract: Tuberculosis is a major cause of death worldwide. Understanding of the pathogenicity of Mycobacterium tuberculosis has been advanced by gene analysis and has led to the identification of genes that are important for intracellular survival in macrophages. One of these genes encodes HsaD, a meta-cleavage product (MCP) hydrolase that catalyzes the hydrolytic cleavage of a carbon-carbon bond in cholesterol metabolism. This paper describes the production of HsaD as a recombinant protein and, following crystallization, the determination of its three-dimensional structure to 2.35 A resolution by X-ray crystallography at the Diamond Light Source in Oxfordshire, England. To the authors' knowledge, this study constitutes the first report of a structure determined at the new synchrotron facility. The volume of the active-site cleft of the HsaD enzyme is more than double the corresponding active-site volumes of related MCP hydrolases involved in the catabolism of aromatic compounds, consistent with the specificity of HsaD for steroids such as cholesterol. Knowledge of the structure of the enzyme facilitates the design of inhibitors.

PubMed: 18097091
DOI: 10.1107/S1744309107065931

実験手法

X-RAY DIFFRACTION (2.35 Å)