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Título: | The structure of dihydrodipicolinate reductase (DapB) from Mycobacterium tuberculosis in three crystal forms |
Autor: | Weiss, Manfred S. | Fecha de publicación: | 2010 | Editor: | Wiley-Blackwell | Citación: | Acta Crystallographica Section D 66(1): 61-72 (2010) | Resumen: | Dihydrodipicolinate reductase (DHDPR, DapB) is an enzyme that belongs to the l-lysine biosynthetic pathway. DHDPR reduces the α,β-unsaturated cyclic imine 2,3-dihydrodipicolinic acid to yield the compound 2,3,4,5-tetrahydrodipicolinic acid in a pyridine nucleotide-dependent reaction. The sub-strate 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. © 2010 International Union of Crystallography Printed in Singapore - all rights reserved. | URI: | http://hdl.handle.net/10261/87473 | DOI: | 10.1107/S0907444909043960 | Identificadores: | doi: 10.1107/S0907444909043960 issn: 0907-4449 e-issn: 1399-0047 |
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