› 2z5l

X-ray diffraction
1.95Å resolution

The first ketoreductase of the tylosin PKS

Released:
DOI: 10.2210/pdb2z5l/pdb
PDB entry 2z5l coloured by chain, front view.
PDB entry 2z5l coloured by chain, side view.
PDB entry 2z5l coloured by chain, top view.
Source organism: Streptomyces fradiae
Primary publication:
A tylosin ketoreductase reveals how chirality is determined in polyketides.
Keatinge-Clay AT
Chem Biol 14 898-908 (2007)
PMID: 17719489

Function and Biology Details

Reaction catalysed: 
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128513 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tylactone synthase starter module and modules 1 & 2 Chain: A
Molecule details ›
Chain: A
Length: 511 amino acids
Theoretical weight: 53.31 KDa
Source organism: Streptomyces fradiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O33954 (Residues: 1962-2451; Coverage: 11%)
Gene name: tylG
Sequence domains: KR domain
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 66.18Å b: 49.81Å c: 68.81Å
α: 90° β: 109.2° γ: 90°
R-values:
R R work R free
0.259 0.259 0.287
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

36 review citations

The biosynthetic logic of polyketide diversity.
Hertweck C. (2009)
35 more

2 mentions without citation

Conformational flexibility of metazoan fatty acid synthase enables catalysis.
Brignole et al. (2009)
1 more