Crystal structure of the TK2203 protein from Thermococcus kodakarensis, a putative extradiol dioxygenase

The TK2203 protein from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1 (262 residues, 29 kDa) is a putative extradiol dioxygenase catalyzing the cleavage of C–C bonds in catechol derivatives. It contains three metal‐binding residues, but has no significant sequence similarity to prote...

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Veröffentlicht in:	Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2016-06, Vol.72 (6), p.427-433
Hauptverfasser:	Nishitani, Yuichi, Simons, Jan-Robert, Kanai, Tamotsu, Atomi, Haruyuki, Miki, Kunio
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence archaea aromatic compound degradation Crystallography, X-Ray homodimer nonhaem iron Oxygenases - chemistry Protein Conformation Research Communications SIRAS Thermococcus - chemistry Thermococcus kodakarensis TK2203
Online-Zugang:	Volltext
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