5HM3
2.25 Angstrom Resolution Crystal Structure of Long-chain-fatty-acid-AMP Ligase FadD32 from Mycobacterium tuberculosis in complex with Inhibitor 5'-O-[(11-phenoxyundecanoyl)sulfamoyl]adenosine
Summary for 5HM3
| Entry DOI | 10.2210/pdb5hm3/pdb |
| Descriptor | Long-chain-fatty-acid--AMP ligase FadD32, 5'-O-[(11-phenoxyundecanoyl)sulfamoyl]adenosine, CHLORIDE ION, ... (7 entities in total) |
| Functional Keywords | long-chain-fatty-acid--amp ligase, fadd32, structural genomics, center for structural genomics of infectious diseases, csgid, ligase-ligase inhibitor complex, ligase/ligase inhibitor |
| Biological source | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Total number of polymer chains | 1 |
| Total formula weight | 73140.36 |
| Authors | Minasov, G.,Warwrzak, Z.,Kuhn, M.L.,Shuvalova, L.,Flores, K.J.,Wilson, D.J.,Grimes, K.D.,Aldrich, C.C.,Anderson, W.A.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2016-01-15, release date: 2016-08-03, Last modification date: 2024-11-13) |
| Primary citation | Kuhn, M.L.,Alexander, E.,Minasov, G.,Page, H.J.,Warwrzak, Z.,Shuvalova, L.,Flores, K.J.,Wilson, D.J.,Shi, C.,Aldrich, C.C.,Anderson, W.F. Structure of the Essential Mtb FadD32 Enzyme: A Promising Drug Target for Treating Tuberculosis. Acs Infect Dis., 2:579-591, 2016 Cited by PubMed Abstract: Mycolic acids are indispensible lipids of (), the causative agent of tuberculosis (TB), and contribute to the distinctive architecture and impermeability of the mycobacterial cell envelope. FadD32 plays a pivotal role in mycolic acid biosynthesis by functionally linking fatty acid synthase (FAS) and polyketide synthase (PKS) biosynthetic pathways. FadD32, a fatty acyl-AMP ligase (FAAL), represents one of the best genetically and chemically validated new TB drug targets. We have determined the three-dimensional crystal structure of FadD32 in complex with a ligand specifically designed to stabilize the catalytically active adenylate-conformation, which provides a foundation for structure-based drug design efforts against this essential protein. The structure also captures the unique interactions of a FAAL-specific insertion sequence and provides insight into the specificity and mechanism of fatty acid transfer. PubMed: 27547819DOI: 10.1021/acsinfecdis.6b00082 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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