1n8i

Biochemical and Structural Studies of Malate Synthase from Mycobacterium tuberculosis

spinqualitylabelsall models 1n8i, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1n8i is a 1 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GLV, MG Related: 1n8w Gene: GLCB ("Bacillus tuberculosis" (Zopf 1883) Klein 1884) Activity: Malate synthase, with EC number 2.3.3.9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [MASZ_MYCTU] Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA (By similarity).[HAMAP-Rule:MF_00641] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Malate synthase

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