› 1xix

X-ray diffraction
2Å resolution

Crystal Structure of Weissella viridescens FemX Form II

Released:
DOI: 10.2210/pdb1xix/pdb
PDB entry 1xix coloured by chain, front view.
PDB entry 1xix coloured by chain, side view.
PDB entry 1xix coloured by chain, top view.
Source organism: Weissella viridescens
Primary publication:
Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens.
Maillard AP, Biarrotte-Sorin S, Villet R, Mesnage S, Bouhss A, Sougakoff W, Mayer C, Arthur M
J Bacteriol 187 3833-8 (2005)
PMID: 15901708

Function and Biology Details

Reaction catalysed: 
L-alanyl-tRNA(Ala) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine = tRNA(Ala) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-N(6)-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190221 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase Chain: A
Molecule details ›
Chain: A
Length: 335 amino acids
Theoretical weight: 38.2 KDa
Source organism: Weissella viridescens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9EY50 (Residues: 2-336; Coverage: 100%)
Gene name: femX
Sequence domains: FemAB family
Structure domains: Aminopeptidase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P21
Unit cell:
a: 42.267Å b: 101.537Å c: 46.714Å
α: 90° β: 103.19° γ: 90°
R-values:
R R work R free
0.193 0.175 0.214
Expression system: Escherichia coli

Quick links

Citations

10 review citations

The biosynthesis of peptidoglycan lipid-linked intermediates.
Bouhss et al. (2008)
9 more

1 mention without citation

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).
Salah Ud-Din et al. (2016)