7LXI
Crystal structure of S-adenosylmethionine-dependent methyltransferase UmaA from Mycobacterium tuberculosis in complex with SAH
Summary for 7LXI
| Entry DOI | 10.2210/pdb7lxi/pdb |
| Descriptor | S-adenosylmethionine-dependent methyltransferase UmaA, HEXAETHYLENE GLYCOL, NITRATE ION, ... (8 entities in total) |
| Functional Keywords | ssgcid, s-adenosylmethionine-dependent methyltransferase, sam-dependent methyltransferase, umaa, mycobacterium tuberculosis, short-chain fatty acid modification, sah, s-adenosyl-l-homocysteine, structural genomics, seattle structural genomics center for infectious disease, transferase |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 1 |
| Total formula weight | 35145.99 |
| Authors | Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2021-03-03, release date: 2021-03-17, Last modification date: 2025-04-09) |
| Primary citation | Teng, S.,Wang, J.,Sroge, C.D.,Abendroth, J.,Lorimer, D.D.,Horanyi, P.S.,Edwards, T.E.,Tillery, L.,Craig, J.K.,Van Voorhis, W.C.,Myler, P.J.,Smith, C.L. Crystal structure of the S-adenosylmethionine-dependent mycolic acid synthase UmaA from Mycobacterium tuberculosis. Acta Crystallogr.,Sect.F, 81:146-154, 2025 Cited by PubMed Abstract: Mycobacterium tuberculosis is a Gram-positive bacillus that causes tuberculosis and is a leading cause of mortality worldwide. This disease is a growing health threat due to the occurrence of multidrug resistance. Mycolic acids are essential for generating cell walls and their modification is important to the virulence and persistence of M. tuberculosis. A family of S-adenosylmethionine-dependent mycolic acid synthases modify mycolic acids and represent promising drug targets. UmaA is currently the least-understood member of this family. This paper describes the crystal structure of UmaA. UmaA is a monomer composed of two domains: a structurally conserved SAM-binding domain and a variable substrate-binding auxiliary domain. Fortuitously, our structure contains a nitrate in the active site, a structural mimic of carbonate, which is a known general base in cyclopropane-adding synthases. Further investigation indicated that the structure of the N-terminus is highly flexible. Finally, we have identified S-adenosyl-N-decyl-aminoethyl as a promising potential inhibitor. PubMed: 40059638DOI: 10.1107/S2053230X25001530 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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