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Crystal structure of the TK2203 protein from Thermococcus kodakarensis , a putative extradiol dioxygenase
Author(s) -
Nishitani Yuichi,
Simons Jan-Robert,
Kanai Tamotsu,
Atomi Haruyuki,
Miki Kunio
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x16006920
Subject(s) - thermococcus , dioxygenase , structural genomics , stereochemistry , chemistry , crystal structure , hyperthermophile , biology , protein structure , biochemistry , enzyme , crystallography , gene , archaea
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 proteins for which structures have been determined. Here, the first crystal structure of the TK2203 protein was determined at 1.41 Å resolution to investigate its functional role. Structure analysis reveals that this protein shares the same fold and catalytic residues as other extradiol dioxygenases, strongly suggesting the same enzymatic activity. Furthermore, the important region contributing to substrate selectivity is discussed.