› 4q1h

X-ray diffraction
1.93Å resolution

Structure and mechanism of a dehydratase/decarboxylase enzyme couple involved in polyketide beta-branching

Released:
DOI: 10.2210/pdb4q1h/pdb
PDB entry 4q1h coloured by chain, front view.
PDB entry 4q1h coloured by chain, side view.
PDB entry 4q1h coloured by chain, top view.
Source organism: Bacillus subtilis subsp. subtilis str. 168
Primary publication:
Structure and mechanism of a dehydratase/decarboxylase enzyme couple involved in polyketide β-methyl branch incorporation.
Nair AV, Robson A, Ackrill TD, Till M, Byrne MJ, Back CR, Tiwari K, Davies JA, Willis CL, Race PR
Sci Rep 10 15323 (2020)
PMID: 32948786

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-216329 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative polyketide biosynthesis enoyl-CoA isomerase PksI Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 268 amino acids
Theoretical weight: 30.08 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
  • Canonical: P40802 (Residues: 1-249; Coverage: 100%)
Gene names: BSU17170, pksI
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand GOL 8 x GOL
Ligand NA 1 x NA
Ligand EPE 1 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 82.89Å b: 84.66Å c: 125.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.149 0.185
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

Structure and mechanism of a dehydratase/decarboxylase enzyme couple involved in polyketide β-methyl branch incorporation.
Nair et al. (2020)