3eag

X-ray diffraction
2.55Å resolution

The crystal structure of UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase (MPL) from Neisseria meningitides

Released:
Source organism: Neisseria meningitidis MC58
Entry authors: Chang C, Hendricks R, Clancy S, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
ATP + UDP-N-acetyl-alpha-D-muramate + L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 326 amino acids
Theoretical weight: 35.89 KDa
Source organism: Neisseria meningitidis MC58
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9JRY9 (Residues: 1-323; Coverage: 71%)
Gene names: NMB1145, NMB1183, mpl, mpl-1, mpl-2
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 65.497Å b: 83.8Å c: 143.838Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.183 0.243
Expression system: Escherichia coli