› 2uvk

X-ray diffraction
1.5Å resolution

Structure of YjhT

Released:
DOI: 10.2210/pdb2uvk/pdb
PDB entry 2uvk coloured by chain, front view.
PDB entry 2uvk coloured by chain, side view.
PDB entry 2uvk coloured by chain, top view.
Source organism: Escherichia coli BL21
Primary publication:
Sialic acid mutarotation is catalyzed by the Escherichia coli beta-propeller protein YjhT.
Severi E, Müller A, Potts JR, Leech A, Williamson D, Wilson KS, Thomas GH
J Biol Chem 283 4841-9 (2008)
PMID: 18063573

Function and Biology Details

Reaction catalysed: 
(1a) N-acetyl-alpha-neuraminate = aceneuramate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153872 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetylneuraminate epimerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 357 amino acids
Theoretical weight: 38.87 KDa
Source organism: Escherichia coli BL21
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P39371 (Residues: 20-368; Coverage: 100%)
Gene names: JW5777, b4310, nanM, yjhT
Sequence domains: Galactose oxidase, central domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 44.758Å b: 105.659Å c: 74.222Å
α: 90° β: 99.95° γ: 90°
R-values:
R R work R free
0.182 0.18 0.219
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Nontypeable Haemophilus influenzae: the role of N-acetyl-5-neuraminic acid in biology.
Apicella MA. (2012)
3 more

3 mentions without citation

Biochemical and structural basis of sialic acid utilization by gut microbes.
Bell et al. (2023)
2 more