5HEE

Crystal structure of the TK2203 protein

5HEE の概要

• エントリーDOI: 10.2210/pdb5hee/pdb
• 分子名称: Putative uncharacterized protein, TK2203 protein, ZINC ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: putative, dioxygenase, oxidoreductase
• 由来する生物種: Thermococcus kodakarensis KOD1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59374.63

構造登録者

Nishitani, Y.,Miki, K. (登録日: 2016-01-06, 公開日: 2016-06-29, 最終更新日: 2024-03-20)

主引用文献

Nishitani, Y.,Simons, J.R.,Kanai, T.,Atomi, H.,Miki, K.
Crystal structure of the TK2203 protein from Thermococcus kodakarensis, a putative extradiol dioxygenase
Acta Crystallogr.,Sect.F, 72:427-433, 2016

PubMed Abstract: 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.

PubMed: 27303894
DOI: 10.1107/S2053230X16006920

実験手法

X-RAY DIFFRACTION (1.41 Å)