3DTF
Structural analysis of mycobacterial branched chain aminotransferase- implications for inhibitor design
Summary for 3DTF
| Entry DOI | 10.2210/pdb3dtf/pdb |
| Related | 3DTG 3DTH |
| Descriptor | Branched-chain amino acid aminotransferase, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | open twisted alpha/beta, aminotransferase, transferase |
| Biological source | Mycobacterium smegmatis |
| Total number of polymer chains | 2 |
| Total formula weight | 81108.74 |
| Authors | Castell, A.,Unge, T. (deposition date: 2008-07-15, release date: 2009-06-23, Last modification date: 2023-11-01) |
| Primary citation | Castell, A.,Mille, C.,Unge, T. Structural analysis of mycobacterial branched-chain aminotransferase: implications for inhibitor design. Acta Crystallogr.,Sect.D, 66:549-557, 2010 Cited by PubMed Abstract: The branched-chain aminotransferase (BCAT) of Mycobacterium tuberculosis has been characterized as being essential to the survival of the bacterium. The enzyme is pyridoxal 5'-phosphate-dependent and belongs to the aminotransferase IIIa subfamily, to which the human BCATs also belong. The overall sequence similarity is high within the subfamily and the sequence identity among the active-site residues is high. In order to identify structurally unique features of M. tuberculosis BCAT, X-ray structural and functional analyses of the closely related BCAT from M. smegmatis were carried out. The crystal structures include the apo form at 2.2 A resolution and a 1.9 A structure of the holo form cocrystallized with the inhibitor O-benzylhydroxylamine (Obe). The analyses highlighted the active-site residues Tyr209 and Gly243 as being structurally unique characteristics of the mycobacterial BCATs relative to the human BCATs. The inhibitory activities of Obe and ammonium sulfate were verified in an inhibition assay. Modelling of the inhibitor Obe in the substrate pocket indicated potential for the design of a mycobacterial-specific inhibitor. PubMed: 20445230DOI: 10.1107/S0907444910004877 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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