› 2ml1

Solution NMR

Solution Structure of AlgE6R1 subunit from the Azotobacter vinelandii Mannuronan C5-epimerase

Released:
DOI: 10.2210/pdb2ml1/pdb
PDB entry 2ml1 coloured by chain, ensemble of 20 models, front view.
PDB entry 2ml1 coloured by chain, ensemble of 20 models, side view.
PDB entry 2ml1 coloured by chain, ensemble of 20 models, top view.
Source organism: Azotobacter vinelandii
Primary publication:
Structural and functional characterization of the R-modules in alginate C-5 epimerases AlgE4 and AlgE6 from Azotobacter vinelandii.
Buchinger E, Knudsen DH, Behrens MA, Pedersen JS, Aarstad OA, Tøndervik A, Valla S, Skjåk-Bræk G, Wimmer R, Aachmann FL
J Biol Chem 289 31382-96 (2014)
PMID: 25266718

Function and Biology Details

Reaction catalysed: 
(Mannuronan)-beta-D-mannuronate = (alginate)-alpha-L-guluronate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-579211 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mannuronan C5-epimerase AlgE6 Chain: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 15.46 KDa
Source organism: Azotobacter vinelandii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ZFH0 (Residues: 382-532; Coverage: 17%)
Gene name: algE6
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand CA 6 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 87%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Enzymatic modifications of exopolysaccharides enhance bacterial persistence.
Whitfield et al. (2015)
2 more

4 mentions without citation

Structural and functional characterization of the R-modules in alginate C-5 epimerases AlgE4 and AlgE6 from Azotobacter vinelandii.
Buchinger et al. (2014)
3 more