2JJE
Crystal structure of T330S mutant of Rv3290c from M. tuberculosis
Summary for 2JJE
| Entry DOI | 10.2210/pdb2jje/pdb |
| Related | 2JJF 2JJG 2JJH |
| Descriptor | L-LYSINE EPSILON AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE (3 entities in total) |
| Functional Keywords | aminotransferase, pyridoxal phosphate, plp, rv3290c, transferase, t330s mutant, lysine amino transferase, mycobacterium tuberculosis |
| Biological source | MYCOBACTERIUM TUBERCULOSIS |
| Total number of polymer chains | 1 |
| Total formula weight | 49302.09 |
| Authors | Tripathi, S.M.,Ramachandran, R. (deposition date: 2008-04-03, release date: 2009-06-30, Last modification date: 2020-01-15) |
| Primary citation | Tripathi, S.M.,Agarwal, A.,Ramachandran, R. Mutational Analysis of Mycobacterium Tuberculosis Lysine Epsilon-Aminotransferase and Inhibitor Co-Crystal Structures, Reveals Distinct Binding Modes. Biochem.Biophys.Res.Commun., 463:154-, 2015 Cited by PubMed Abstract: Lysine ɛ-aminotransferase (LAT) converts lysine to α-aminoadipate-δ-semialdehyde in a PLP-mediated reaction. We mutated active-site T330, N328 and E243, and structurally rationalized their properties. T330A and T330S mutants cannot bind PLP and are inactive. N328A although inactive, binds to PLP. E243A retains activity, but binds α-ketoglutarate in a different conformation. We had earlier identified 2-aminomethyl piperidine derivative as a LAT inhibitor. The co-crystal structure reveals that it mimics binding of C5 substrates and exhibits two binding modes. E243, that shields R422 in the apo enzyme, exhibits conformational changes to permit the binding of the inhibitor in one of the binding modes. Structure-based analysis of bound water in the active site suggests optimization strategies for synthesis of improved inhibitors. PubMed: 26003725DOI: 10.1016/J.BBRC.2015.05.055 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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