3QHX
Crystal Structure of Cystathionine gamma-synthase MetB (Cgs) from Mycobacterium ulcerans Agy99 bound to HEPES
Summary for 3QHX
Entry DOI | 10.2210/pdb3qhx/pdb |
Related | 3QI6 |
Descriptor | Cystathionine gamma-synthase MetB (Cgs), SULFATE ION, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (6 entities in total) |
Functional Keywords | structural genomics, seattle structural genomics center for infectious disease, ssgcid, cgs_like, aat_i superfamily, llp, plp, lyase |
Biological source | Mycobacterium ulcerans |
Total number of polymer chains | 4 |
Total formula weight | 166095.14 |
Authors | Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2011-01-26, release date: 2011-03-02, Last modification date: 2023-12-06) |
Primary citation | Clifton, M.C.,Abendroth, J.,Edwards, T.E.,Leibly, D.J.,Gillespie, A.K.,Ferrell, M.,Dieterich, S.H.,Exley, I.,Staker, B.L.,Myler, P.J.,Van Voorhis, W.C.,Stewart, L.J. Structure of the cystathionine [gamma]-synthase MetB from Mycobacterium ulcerans Acta Crystallogr.,Sect.F, 67:1154-1158, 2011 Cited by PubMed Abstract: Cystathionine γ-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 Å 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. PubMed: 21904066DOI: 10.1107/S1744309111029575 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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