1YL7
the crystal structure of Mycobacterium tuberculosis dihydrodipicolinate reductase (Rv2773c) in complex with NADH (crystal form C)
Summary for 1YL7
| Entry DOI | 10.2210/pdb1yl7/pdb |
| Related | 1YL5 1YL6 |
| Descriptor | Dihydrodipicolinate reductase, MAGNESIUM ION, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | lysine biosynthesis, dihydrodipicolinate, reductase, nadh, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, oxidoreductase |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 8 |
| Total formula weight | 211095.28 |
| Authors | Janowski, R.,Kefala, G.,Weiss, M.S.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2005-01-19, release date: 2006-01-17, Last modification date: 2023-08-23) |
| Primary citation | Janowski, R.,Kefala, G.,Weiss, M.S. The structure of dihydrodipicolinate reductase (DapB) from Mycobacterium tuberculosis in three crystal forms. Acta Crystallogr.,Sect.D, 66:61-72, 2010 Cited by PubMed Abstract: Dihydrodipicolinate reductase (DHDPR, DapB) is an enzyme that belongs to the L-lysine biosynthetic pathway. DHDPR reduces the alpha,beta-unsaturated cyclic imine 2,3-dihydrodipicolinic acid to yield the compound 2,3,4,5-tetrahydrodipicolinic acid in a pyridine nucleotide-dependent reaction. The substrate of this reaction is the unstable product of the preceding enzyme dihydrodipicolinate synthase (DHDPS, DapA). Here, the structure of apo-DHDPR from Mycobacterium tuberculosis is reported in two orthorhombic crystal forms, as well as the structure of DHDPR from M. tuberculosis in complex with NADH in a monoclinic crystal form. A comparison of the results with previously solved structures of this enzyme shows that DHDPR undergoes a major conformational change upon binding of its cofactor. This conformational change can be interpreted as one of the low-frequency normal modes of the structure. PubMed: 20057050DOI: 10.1107/S0907444909043960 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.34 Å) |
Structure validation
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