› 2wo5

X-ray diffraction
2.2Å resolution

Structure of wild type E. coli N-acetylneuraminic acid lyase in space group P21 crystal form I

Released:
DOI: 10.2210/pdb2wo5/pdb
PDB entry 2wo5 coloured by chain, front view.
PDB entry 2wo5 coloured by chain, side view.
PDB entry 2wo5 coloured by chain, top view.
Source organism: Escherichia coli BL21(DE3)
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
OpenAccess logo 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: 304 amino acids
Theoretical weight: 33.58 KDa
Source organism: Escherichia coli BL21(DE3)
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6L4 (Residues: 2-297; Coverage: 100%)
Gene names: JW3194, b3225, nanA, npl
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P21
Unit cell:
a: 54.795Å b: 142.167Å c: 84.18Å
α: 90° β: 109.01° γ: 90°
R-values:
R R work R free
0.214 0.211 0.272
Expression system: Escherichia coli

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Citations

1 review citation

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

5 mentions without citation

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Georgescauld et al. (2014)
4 more