› 4axv

X-ray diffraction
2.17Å resolution

Biochemical and structural characterization of the MpaA amidase as part of a conserved scavenging pathway for peptidoglycan derived peptides in gamma-proteobacteria

Released:
DOI: 10.2210/pdb4axv/pdb
PDB entry 4axv coloured by chain, front view.
PDB entry 4axv coloured by chain, side view.
PDB entry 4axv coloured by chain, top view.
Source organism: Vibrio campbellii CAIM 519 = NBRC 15631 = ATCC 25920
Primary publication:
MpaA is a murein-tripeptide-specific zinc carboxypeptidase that functions as part of a catabolic pathway for peptidoglycan-derived peptides in γ-proteobacteria.
Maqbool A, Hervé M, Mengin-Lecreulx D, Wilkinson AJ, Thomas GH
Biochem J 448 329-41 (2012)
PMID: 22970852

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-108377 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Murein peptide amidase A Chain: A
Molecule details ›
Chain: A
Length: 243 amino acids
Theoretical weight: 26.93 KDa
Source organism: Vibrio campbellii CAIM 519 = NBRC 15631 = ATCC 25920
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A7N805 (Residues: 14-248; Coverage: 95%)
Gene names: VIBHAR_07057, mpaA
Sequence domains: Succinylglutamate desuccinylase / Aspartoacylase family
Structure domains: Zn peptidases

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand EDO 1 x EDO
1 modified residue:
Ligand MSE 2 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P6522
Unit cell:
a: 73.6Å b: 73.6Å c: 208.71Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.196 0.233
Expression system: Escherichia coli BL21

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Citations

3 review citations

Fortifying the wall: synthesis, regulation and degradation of bacterial peptidoglycan.
Sobhanifar et al. (2013)
2 more