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Publication Abstract from PubMed

Cystathionine gamma-synthase (CGS) is a transulfurication enzyme that catalyzes the first specific step in L-methionine biosynthesis by the reaction of O(4)-succinyl-L-homoserine and L-cysteine to produce L-cystathionine and succinate. Controlling the first step in L-methionine biosythesis, CGS is an excellent potential drug target. Mycobacterium ulcerans is a slow-growing mycobacterium that is the third most common form of mycobacterial infection, mainly infecting people in Africa, Australia and Southeast Asia. Infected patients display a variety of skin ailments ranging from indolent non-ulcerated lesions as well as ulcerated lesions. Here, the crystal structure of CGS from M. ulcerans covalently linked to the cofactor pyridoxal phosphate (PLP) is reported at 1.9 A resolution. A second structure contains PLP as well as a highly ordered HEPES molecule in the active site acting as a pseudo-ligand. These results present the first structure of a CGS from a mycobacterium and allow comparison with other CGS enzymes. This is also the first structure reported from the pathogen M. ulcerans.

Structure of the cystathionine gamma-synthase MetB from Mycobacterium ulcerans.,Clifton MC, Abendroth J, Edwards TE, Leibly DJ, Gillespie AK, Ferrell M, Dieterich SH, Exley I, Staker BL, Myler PJ, Van Voorhis WC, Stewart LJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt 9):1154-8., Epub 2011 Aug 16. PMID:21904066^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.