2GQ3

mycobacterium tuberculosis malate synthase in complex with magnesium, malate, and coenzyme A

2GQ3 の概要

• エントリーDOI: 10.2210/pdb2gq3/pdb
• 分子名称: Malate synthase G, MAGNESIUM ION, D-MALATE, ... (6 entities in total)
• 機能のキーワード: tim barrel, coenzyme a, transferase
• 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: 160052.38

構造登録者

Anstrom, D.M.,Remington, S.J. (登録日: 2006-04-19, 公開日: 2006-08-15, 最終更新日: 2023-08-30)

主引用文献

Anstrom, D.M.,Remington, S.J.
The product complex of M. tuberculosis malate synthase revisited.
Protein Sci., 15:2002-2007, 2006

PubMed Abstract: Enzymes of the glyoxylate shunt have been implicated as virulence factors in several pathogenic organisms, notably Mycobacterium tuberculosis and Candida albicans. Malate synthase has thus emerged as a promising target for design of anti-microbial agents. For this effort, it is essential to have reliable models for enzyme:substrate complexes. A 2.7 Angstroms resolution crystal structure for M. tuberculosis malate synthase in the ternary complex with magnesium, malate, and coenzyme A has been previously described. However, some unusual aspects of malate and Mg(++) binding prompted an independent determination of the structure at 2.3 Angstroms resolution, in the presence of saturating concentrations of malate. The electron density map of the complex reveals the position and conformation of coenzyme A to be unchanged from that found in the previous study. However, the coordination of Mg(++) and orientation of bound malate within the active site are different. The revised position of bound malate is consistent with a reaction mechanism that does not require reorientation of the electrophilic substrate during the catalytic cycle, while the revised Mg(++) coordination is octahedral, as expected. The results should be useful in the design of malate synthase inhibitors.

PubMed: 16877713
DOI: 10.1110/ps.062300206

実験手法

X-RAY DIFFRACTION (2.3 Å)