1n8w

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spinqualitylabelsall models 1n8w, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Biochemical and Structural Studies of Malate Synthase from Mycobacterium tuberculosis

Overview

Establishment or maintenance of a persistent infection by Mycobacterium, tuberculosis requires the glyoxylate pathway. This is a bypass of the, tricarboxylic acid cycle in which isocitrate lyase and malate synthase, (GlcB) catalyze the net incorporation of carbon during growth of, microorganisms on acetate or fatty acids as the primary carbon source. The, glcB gene from M. tuberculosis, which encodes malate synthase, was cloned, and GlcB was expressed in Escherichia coli. The influence of media, conditions on expression in M. tuberculosis indicated that this enzyme is, regulated differentially to isocitrate lyase. Purified GlcB had K(m), values of 57 and 30 microm for its substrates glyoxylate and acetyl, coenzyme A, respectively, and was inhibited by bromopyruvate, oxalate, and, phosphoenolpyruvate. The GlcB structure was solved to 2.1-A resolution in, the presence of glyoxylate and magnesium. We also report the structure of, GlcB in complex with the products of the reaction, coenzyme A and malate, solved to 2.7-A resolution. Coenzyme A binds in a bent conformation, and, the details of its interactions are described, together with implications, on the enzyme mechanism.

About this Structure

1N8W is a Single protein structure of sequence from Mycobacterium tuberculosis with MG, SO4, MLT, COA and GLV as ligands. Active as Malate synthase, with EC number 2.3.3.9 Full crystallographic information is available from OCA.

Reference

Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis., Smith CV, Huang CC, Miczak A, Russell DG, Sacchettini JC, Honer zu Bentrup K, J Biol Chem. 2003 Jan 17;278(3):1735-43. Epub 2002 Oct 21. PMID:12393860

Page seeded by OCA on Tue Nov 20 22:03:42 2007