› 2wnn

X-ray diffraction
1.65Å resolution

Structure of wild type E. coli N-acetylneuraminic acid lyase in complex with pyruvate in space group P21

Released:
DOI: 10.2210/pdb2wnn/pdb
PDB entry 2wnn coloured by chain, front view.
PDB entry 2wnn coloured by chain, side view.
PDB entry 2wnn coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural insights into substrate specificity in variants of N-acetylneuraminic Acid lyase produced by directed evolution.
Campeotto I, Bolt AH, Harman TA, Dennis C, Trinh CH, Phillips SE, Nelson A, Pearson AR, Berry A
J Mol Biol 404 56-69 (2010)
PMID: 20826162

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: 33.6 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
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 NA 1 x NA
Ligand 1PE 3 x 1PE
1 modified residue:
Ligand KPI 4 x KPI

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21
Unit cell:
a: 54.693Å b: 142.456Å c: 83.626Å
α: 90° β: 109.16° γ: 90°
R-values:
R R work R free
0.212 0.21 0.249
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Engineering specialized metabolic pathways--is there a room for enzyme improvements?
Bar-Even et al. (2013)
10 other articles

6 mentions without citation

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Bell et al. (2023)
5 more