› 3u49

X-ray diffraction
1.75Å resolution

Crystal structure of YwfH, NADPH dependent reductase involved in Bacilysin biosynthesis

Released:
DOI: 10.2210/pdb3u49/pdb
PDB entry 3u49 coloured by chain, front view.
PDB entry 3u49 coloured by chain, side view.
PDB entry 3u49 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structural insights into the role of Bacillus subtilis YwfH (BacG) in tetrahydrotyrosine synthesis.
Rajavel M, Perinbam K, Gopal B
Acta Crystallogr D Biol Crystallogr 69 324-32 (2013)
PMID: 23519407

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153919 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADPH-dependent reductase BacG Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 281 amino acids
Theoretical weight: 30.47 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P39644 (Residues: 1-259; Coverage: 100%)
Gene names: BSU37680, bacG, ipa-86r, ywfH
Sequence domains: Enoyl-(Acyl carrier protein) reductase
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: ESRF BEAMLINE BM14
Spacegroup: P21
Unit cell:
a: 64.85Å b: 136.99Å c: 66.7Å
α: 90° β: 117.99° γ: 90°
R-values:
R R work R free
0.19 0.189 0.222
Expression system: Escherichia coli

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Citations

3 citation in other articles

Prevalence of an Intestinal ST40 Enterococcus faecalis over Other E. faecalis Strains in the Gut Environment of Mice Fed Different High Fat Diets.
Sánchez et al. (2020)
2 more

1 mention without citation

Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of AerF from Microcystis aeruginosa, a putative reductase participating in aeruginosin biosynthesis.
Ding et al. (2015)