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1yl6
From Proteopedia
| 1yl6, resolution 2.90Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||||
| Ligands: | |||||||||
| Gene: | dapB (Mycobacterium tuberculosis) | ||||||||
| Activity: | Dihydrodipicolinate reductase, with EC number 1.3.1.26 | ||||||||
| Related: | 1yl5, 1yl7 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB, TOPSAN | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
crystal structure of Mycobacterium tuberculosis dihydrodipicolinate reductase (Rv2773c) (crystal form B)
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
Categories: Dihydrodipicolinate reductase | Mycobacterium tuberculosis | Janowski, R. | Kefala, G. | TBSGC, TB Structural Genomics Consortium. | Weiss, M S. | Dihydrodipicolinate | Lysine biosynthesis | Nadh | Oxidoreductase | Protein structure initiative | Psi | Reductase | Structural genomic | Tb structural genomics consortium | Tbsgc

