Literature summary for 1.14.11.55 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Virgibacillus salexigens

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Organism	UniProt	Comment	Textmining
Virgibacillus salexigens	Q2TDY4	-	-

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Release 2023.1 (January 2023)