› 8ayd

X-ray diffraction
2.8Å resolution

Anammox-specific FabZ from the annamox bacterium Kuenenia stuttgartiensis

Released:
DOI: 10.2210/pdb8ayd/pdb
PDB entry 8ayd coloured by chain, front view.
PDB entry 8ayd coloured by chain, side view.
PDB entry 8ayd coloured by chain, top view.
Source organism: Candidatus Kuenenia stuttgartiensis
Primary publication:
Structures of an unusual 3-hydroxyacyl dehydratase (FabZ) from a ladderane-producing organism with an unexpected substrate preference.
Dietl A, Wellach K, Mahadevan P, Mertes N, Winter S, Kutsch T, Walz C, Schlichting I, Fabritz S, Barends TM
J Biol Chem 104602 (2023)
PMID: 36907440

Function and Biology Details

Reaction catalysed: 
A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-214953 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Strongly similar to hydroxymyristoyl acyl carrier protein dehydratase Chains: AA, BA, CA
Molecule details ›
Chains: AA, BA, CA
Length: 156 amino acids
Theoretical weight: 17.47 KDa
Source organism: Candidatus Kuenenia stuttgartiensis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q1Q2X5 (Residues: 3-149; Coverage: 99%)
Gene names: KSMBR1_3473, KsCSTR_20940, fabZ, fabZ_2, kuste3604
Sequence domains: FabA-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P4322
Unit cell:
a: 75.35Å b: 75.35Å c: 179.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.254 0.252 0.284
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

Structures of an unusual 3-hydroxyacyl dehydratase (FabZ) from a ladderane-producing organism with an unexpected substrate preference.
Dietl et al. (2023)