› 3zu3

X-ray diffraction
1.8Å resolution

Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH (MR, cleaved Histag)

Released:
DOI: 10.2210/pdb3zu3/pdb
PDB entry 3zu3 coloured by chain, front view.
PDB entry 3zu3 coloured by chain, side view.
PDB entry 3zu3 coloured by chain, top view.
Source organism: Yersinia pestis CO92
Primary publication:
Structure of the Yersinia pestis FabV enoyl-ACP reductase and its interaction with two 2-pyridone inhibitors.
Hirschbeck MW, Kuper J, Lu H, Liu N, Neckles C, Shah S, Wagner S, Sotriffer CA, Tonge PJ, Kisker C
Structure 20 89-100 (2012)
PMID: 22244758

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187180 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] Chain: A
Molecule details ›
Chain: A
Length: 405 amino acids
Theoretical weight: 44.03 KDa
Source organism: Yersinia pestis CO92
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8Z9U1 (Residues: 1-399; Coverage: 100%)
Gene names: YPO4104, YP_4011, fabV, y4119
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAI 1 x NAI
2 bound ligands:
Ligand GOL 4 x GOL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P3121
Unit cell:
a: 102.16Å b: 102.16Å c: 84.761Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 0.168 0.212
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Bacterial lipids: metabolism and membrane homeostasis.
Parsons et al. (2013)
3 more

3 mentions without citation

Bacterial Enoyl-Reductases: The Ever-Growing List of Fabs, Their Mechanisms and Inhibition.
Hopf et al. (2022)
2 more