2gq3
From Proteopedia
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mycobacterium tuberculosis malate synthase in complex with magnesium, malate, and coenzyme A
Overview
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.
About this Structure
2GQ3 is a Single protein structure of sequence from Mycobacterium tuberculosis with MG, MLT, COA and EPE as ligands. Active as Malate synthase, with EC number 2.3.3.9 Full crystallographic information is available from OCA.
Reference
The product complex of M. tuberculosis malate synthase revisited., Anstrom DM, Remington SJ, Protein Sci. 2006 Aug;15(8):2002-7. PMID:16877713
Page seeded by OCA on Wed Nov 21 11:20:14 2007
Categories: Malate synthase | Mycobacterium tuberculosis | Single protein | Anstrom, D.M. | Remington, S.J. | COA | EPE | MG | MLT | Coenzyme a | Tim barrel
