1YL5

Crystal structure of Mycobacterium tuberculosis dihydrodipicolinate reductase (RV2773C) (crystal form A)

Summary for 1YL5

• Entry DOI: 10.2210/pdb1yl5/pdb
• Related: 1YL6 1YL7
• Descriptor: Dihydrodipicolinate reductase, MAGNESIUM ION (3 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: 2
• Total formula weight: 51859.64

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

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: 20057050
DOI: 10.1107/S0907444909043960

Experimental method

X-RAY DIFFRACTION (2.3 Å)