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Literature summary for 6.1.1.3 extracted from

  • Dwivedi, S.; Kruparani, S.P.; Sankaranarayanan, R.
    Cloning, expression, purification, crystallization and preliminary X-ray crystallographic investigations of a unique editing domain from archaebacteria (2004), Acta Crystallogr. Sect. D, 60, 1662-1664.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination of residues 1-183, expression in Escherichia coli strain BL21(DE3) Pyrococcus abyssi

Crystallization (Commentary)

Crystallization (Comment) Organism
purified ultrafiltrated recombinant residues 1-183, hanging drop vapour diffusion method, protein solution, containing 50 mM Tris-HCl, pH 7.5, and 50 mM NaCl, drops of varying volumes against 0.75 ml reservoir solution, at room temperature or at 4°C, preliminary X-ray diffraction for structure determination at 1.95 A resolution Pyrococcus abyssi

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-threonine + tRNAThr Pyrococcus abyssi
-
AMP + diphosphate + L-threonyl-tRNAThr
-
r

Organism

Organism UniProt Comment Textmining
Pyrococcus abyssi
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant residues 1-183 from Escherichia coli strain BL21(DE3) by ion exchange chromatography, ammonium sulfate fractionation and gel filtration to homogeneity Pyrococcus abyssi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-threonine + tRNAThr
-
Pyrococcus abyssi AMP + diphosphate + L-threonyl-tRNAThr
-
r
ATP + L-threonine + tRNAThr editing mechanism Pyrococcus abyssi AMP + diphosphate + L-threonyl-tRNAThr
-
r

Synonyms

Synonyms Comment Organism
Threonyl-tRNA synthetase
-
Pyrococcus abyssi
ThrRS
-
Pyrococcus abyssi

Cofactor

Cofactor Comment Organism Structure
AMP
-
Pyrococcus abyssi
ATP
-
Pyrococcus abyssi