› 4bii

X-ray diffraction
1.95Å resolution

How nature bridges the gap: Crystallographic elucidation of pyridomycin binding to InhA

Released:
DOI: 10.2210/pdb4bii/pdb
PDB entry 4bii coloured by chain, front view.
PDB entry 4bii coloured by chain, side view.
PDB entry 4bii coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Pyridomycin bridges the NADH- and substrate-binding pockets of the enoyl reductase InhA.
Hartkoorn RC, Pojer F, Read JA, Gingell H, Neres J, Horlacher OP, Altmann KH, Cole ST
Nat Chem Biol 10 96-8 (2014)
PMID: 24292073

Function and Biology Details

Reaction catalysed: 
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161512 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 269 amino acids
Theoretical weight: 28.55 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WGR1 (Residues: 1-269; Coverage: 100%)
Gene names: MTCY277.05, Rv1484, inhA
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 3 x NAD
1 bound ligand:
Ligand PYW 3 x PYW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 64.852Å b: 110.285Å c: 67.519Å
α: 90° β: 98.21° γ: 90°
R-values:
R R work R free
0.179 0.178 0.205
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

12 review citations

New agents for the treatment of drug-resistant Mycobacterium tuberculosis.
Hoagland et al. (2016)
11 more

24 mentions without citation

Using modern tools to probe the structure-function relationship of fatty acid synthases.
Finzel et al. (2015)
23 more