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1yl6

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1yl6, resolution 2.90Å ()
Sites: and
Ligands:
Gene: dapB (Mycobacterium tuberculosis)
Activity: Dihydrodipicolinate reductase, with EC number 1.3.1.26
Related: 1yl5, 1yl7
Resources: FirstGlance, OCA, PDBsum, RCSB, TOPSAN
Coordinates: save as pdb, mmCIF, xml



crystal structure of Mycobacterium tuberculosis dihydrodipicolinate reductase (Rv2773c) (crystal form B)

Publication Abstract from PubMed

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.

The structure of dihydrodipicolinate reductase (DapB) from Mycobacterium tuberculosis in three crystal forms., Janowski R, Kefala G, Weiss MS, Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):61-72. Epub 2009, Dec 21. PMID:20057050

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1YL6 is a 2 chains structure with sequences from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

  • Janowski R, Kefala G, Weiss MS. The structure of dihydrodipicolinate reductase (DapB) from Mycobacterium tuberculosis in three crystal forms. Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):61-72. Epub 2009, Dec 21. PMID:20057050 doi:10.1107/S0907444909043960

Page seeded by OCA on Wed Jan 27 19:48:24 2010

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