› 4f6c

X-ray diffraction
2.81Å resolution

Crystal structure of Aureusimine biosynthetic cluster reductase domain

Released:
DOI: 10.2210/pdb4f6c/pdb
PDB entry 4f6c coloured by chain, front view.
PDB entry 4f6c coloured by chain, side view.
PDB entry 4f6c coloured by chain, top view.
Source organism: Staphylococcus aureus subsp. aureus Mu50
Primary publication:
Heterologous expression and structural characterisation of a pyrazinone natural product assembly line.
Wyatt MA, Mok MC, Junop M, Magarvey NA
Chembiochem 13 2408-15 (2012)
PMID: 23070851

Function and Biology Details

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-101994 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative long chain fatty acid-CoA ligase VraA Chains: A, B
Molecule details ›
Chains: A, B
Length: 427 amino acids
Theoretical weight: 49.55 KDa
Source organism: Staphylococcus aureus subsp. aureus Mu50
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H3JX00 (Residues: 2010-2391; Coverage: 16%)
Gene name: SAV0179
Sequence domains: Male sterility protein
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 38 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 105.699Å b: 106.446Å c: 124.878Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.243
Expression system: Escherichia coli

Quick links

Citations

11 review citations

The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life.
Beld et al. (2014)
10 more

3 mentions without citation

Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.
Patel et al. (2023)
2 more