› 5tek

X-ray diffraction
2.01Å resolution

Apo Structure of 4-Hydroxy-tetrahydrodipicolinate Reductase from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb5tek/pdb
Model geometry
Fit model/data
PDB entry 5tek coloured by chain, front view.
PDB entry 5tek coloured by chain, side view.
PDB entry 5tek coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Ra
Primary publication:
Comparative structural and mechanistic studies of 4-hydroxy-tetrahydrodipicolinate reductases from Mycobacterium tuberculosis and Vibrio vulnificus.
Pote S, Kachhap S, Mank NJ, Daneshian L, Klapper V, Pye S, Arnette AK, Shimizu LS, Borowski T, Chruszcz M
Biochim Biophys Acta Gen Subj 1865 129750 (2021)
PMID: 32980502

Function and Biology Details

Reaction catalysed: 
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)(+) + H(2)O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107745 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-tetrahydrodipicolinate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 250 amino acids
Theoretical weight: 26.18 KDa
Source organism: Mycobacterium tuberculosis H37Ra
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A5U6C6 (Residues: 1-245; Coverage: 100%)
Gene names: MRA_2798, dapB
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand CL 3 x CL
Ligand NA 2 x NA
Ligand PG4 2 x PG4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21212
Unit cell:
a: 60.569Å b: 122.607Å c: 80.846Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.192 0.217
Expression system: Escherichia coli BL21(DE3)

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Citations

2 mentions without citation

Crystal structure of dihydrodipicolinate reductase (PaDHDPR) from Paenisporosarcina sp. TG-14: structural basis for NADPH preference as a cofactor.
Lee et al. (2018)
1 more