› 2wkj

X-ray diffraction
1.45Å resolution

Crystal structure of the E192N mutant of E. Coli N-acetylneuraminic acid lyase in complex with pyruvate at 1.45A resolution in space group P212121

Released:
DOI: 10.2210/pdb2wkj/pdb
PDB entry 2wkj coloured by chain, front view.
PDB entry 2wkj coloured by chain, side view.
PDB entry 2wkj coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of an Escherichia coli N-acetyl-D-neuraminic acid lyase mutant, E192N, in complex with pyruvate at 1.45 angstrom resolution.
Campeotto I, Carr SB, Trinh CH, Nelson AS, Berry A, Phillips SE, Pearson AR
Acta Crystallogr Sect F Struct Biol Cryst Commun 65 1088-90 (2009)
PMID: 19923724

Function and Biology Details

Reaction catalysed: 
Aceneneuramate = N-acetyl-D-mannosamine + pyruvate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141379 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetylneuraminate lyase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 303 amino acids
Theoretical weight: 33.58 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6L4 (Residues: 2-296; Coverage: 99%)
Gene names: JW3194, b3225, nanA, npl
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand 1PE 2 x 1PE
Ligand PYR 2 x PYR
1 modified residue:
Ligand KPI 4 x KPI

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 78.329Å b: 108.049Å c: 148.309Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.167 0.189
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Molecular characterization of a novel N-acetylneuraminate lyase from Lactobacillus plantarum WCFS1.
Sánchez-Carrón et al. (2011)
1 more

4 mentions without citation

Structural insights into substrate specificity in variants of N-acetylneuraminic Acid lyase produced by directed evolution.
Campeotto et al. (2010)
3 more