› 3o9p

X-ray diffraction
2.07Å resolution

The structure of the Escherichia coli murein tripeptide binding protein MppA

Released:
DOI: 10.2210/pdb3o9p/pdb
PDB entry 3o9p coloured by chain, front view.
PDB entry 3o9p coloured by chain, side view.
PDB entry 3o9p coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Compensating stereochemical changes allow murein tripeptide to be accommodated in a conventional peptide-binding protein.
Maqbool A, Levdikov VM, Blagova EV, Hervé M, Horler RS, Wilkinson AJ, Thomas GH
J Biol Chem 286 31512-21 (2011)
PMID: 21705338

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-160155 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Periplasmic murein peptide-binding protein MppA Chain: A
Molecule details ›
Chain: A
Length: 519 amino acids
Theoretical weight: 58.04 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P77348 (Residues: 23-537; Coverage: 100%)
Gene names: JW1322, b1329, mppA, ynaH
Sequence domains: Bacterial extracellular solute-binding proteins, family 5 Middle
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MHI 1 x MHI
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P6
Unit cell:
a: 165.074Å b: 165.074Å c: 38.167Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.172 0.218
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Messenger functions of the bacterial cell wall-derived muropeptides.
Boudreau et al. (2012)
2 more

3 mentions without citation

Compensating stereochemical changes allow murein tripeptide to be accommodated in a conventional peptide-binding protein.
Maqbool et al. (2011)
2 more