Literature summary extracted from
Reuter, K.; Pittelkow, M.; Bursy, J.; Heine, A.; Craan, T.; Bremer, E.
Synthesis of 5-hydroxyectoine from ectoine: crystal structure of the non-heme iron(II) and 2-oxoglutarate-dependent dioxygenase EctD (2010), PLoS ONE, 5, e10647.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.14.11.55 |
expression in Escherichia coli |
Virgibacillus salexigens |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.14.11.55 |
crystal structure in complex with Fe3+ at a resolution of 1.85 A. The core of the EctD structure consists of a double-stranded beta-helix forming the main portion of the active-site of the enzyme. The positioning of the iron ligand in the active site is mediated by an evolutionarily conserved 2-His-1-carboxylate iron-binding motif. The side chains of the three residues forming this iron-binding site protrude into a deep cavity in the EctD structure that also harbours the 2-oxoglutarate cosubstrate-binding site |
Virgibacillus salexigens |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.14.11.55 |
Virgibacillus salexigens |
Q2TDY4 |
- |
- |