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1.14.11.55: ectoine hydroxylase

This is an abbreviated version!
For detailed information about ectoine hydroxylase, go to the full flat file.

Word Map on EC 1.14.11.55

Reaction

ectoine
+
2-oxoglutarate
 +
O2
=
5-hydroxyectoine
 +
succinate
 +
CO2

Synonyms

Csal_3003, ectD, EctE, ectoine dioxygenase, HELO_4008, REctD, Sala_2952, SCATT_10620, ThpD

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
                1.14.11.55 ectoine hydroxylase

Crystallization

Crystallization on EC 1.14.11.55 - ectoine hydroxylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.4 A resolution, space group P1, with unit-cell parameters a 45.18 A, b 58.87 A, c 68.81 A, alpha 77.48 degrees, beta 86.03 degrees, gamma 66.97 degrees. The asymmetric unit contains two molecules with a Mattews coefficient of about 2.44 A3/Da and a solvent content of 49.53%
Alkalihalophilus pseudofirmus
apo-enzyme crystallizes in space group C2221, the iron-supplemented form displays a P212121 symmetry. The apo form contains one monomer per asymmetric unit whereas the Fe-supplemented form contains a dimer
crystal structure in its apo-form, in complex with iron, and in complex with iron, cosubstrate 2-oxoglutarate, and 5-hydroxyectoine. The iron and 2-oxoglutarate ligands are bound within the active site in a fashion similar to that found in other members of the dioxygenase superfamily. 5-Hydroxyectoine is bound by residues residues His144, His245, and Asp146 forming the 2-His-1-carboxylate facial triad
modeling and docking of different substrates into the crystal structure. The spatial positioning of homoectoine and its hydroxylated derivative in the reaction chamber are super-imposable with that of the 5-hydroxyectoine molecule
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
structural comparison, molecular dynamics simulations, and site-directed mutagenesis suggest the positioning of the iron, ectoine, and 2-oxoglutarate ligands in close proximity to each other and with a spatial orientation that will allow the region-selective and stereo-specific hydroxylation of (4S)-ectoine to (4S,5S)-5-hydroxyectoine
to 1.9 A resolution, and comparison of iron-bound and apo structure. The iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/E…H motif, the so-called 2-His-1-carboxylate facial triad