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
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1.14.11.55
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2-oxoglutarate-dependent
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halophil
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5-hydroxyectoine
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halomonas
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salexigens
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ironii
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non-heme-containing
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hydroxylases
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alaskensis
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sphingopyxis
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elongata
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stereo-specific
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osmostress
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mechanosensitive
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tetrahydropyrimidine
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ectabc
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stutzeri
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osmolarity
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virgibacillus
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co-substrate
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halotolerant
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maritimus
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chassis
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salina
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region-selective
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thermoregulated
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nitrosopumilus
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chromohalobacter
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thermoprotection
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alkaliphilic
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hydrothermalis
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sitting-drop
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synthesis
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extremophiles
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prop
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apo-form
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monosodium
- 1.14.11.55
-
2-oxoglutarate-dependent
-
halophil
- 5-hydroxyectoine
-
halomonas
- salexigens
-
ironii
-
non-heme-containing
- hydroxylases
- alaskensis
-
sphingopyxis
- elongata
-
stereo-specific
-
osmostress
-
mechanosensitive
-
tetrahydropyrimidine
-
ectabc
- stutzeri
-
osmolarity
-
virgibacillus
-
co-substrate
-
halotolerant
- maritimus
-
chassis
- salina
-
region-selective
-
thermoregulated
- nitrosopumilus
-
chromohalobacter
-
thermoprotection
-
alkaliphilic
- hydrothermalis
-
sitting-drop
- synthesis
-
extremophiles
-
prop
-
apo-form
-
monosodium
Reaction
Synonyms
Csal_3003, ectD, EctE, ectoine dioxygenase, HELO_4008, REctD, Sala_2952, SCATT_10620, ThpD
ECTree
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Crystallization
Crystallization on EC 1.14.11.55 - ectoine hydroxylase
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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