6BDJ

Crystal structure of dioxygenase Tetur07g02040

6BDJ の概要

• エントリーDOI: 10.2210/pdb6bdj/pdb
• 分子名称: Tetur07g02040, FE (III) ION (3 entities in total)
• 機能のキーワード: dioxygenase, two-spotted spider mite, agricultural pest, detoxification, metal binding protein
• 由来する生物種: Tetranychus urticae (Two-spotted spider mite)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55978.30

構造登録者

Daneshian, L.,Schlachter, C.R.,Chruszcz, M. (登録日: 2017-10-23, 公開日: 2018-11-14, 最終更新日: 2024-11-06)

主引用文献

Schlachter, C.R.,Daneshian, L.,Amaya, J.,Klapper, V.,Wybouw, N.,Borowski, T.,Van Leeuwen, T.,Grbic, V.,Grbic, M.,Makris, T.M.,Chruszcz, M.
Structural and functional characterization of an intradiol ring-cleavage dioxygenase from the polyphagous spider mite herbivore Tetranychus urticae Koch.
Insect Biochem.Mol.Biol., 107:19-30, 2019

PubMed Abstract: Genome analyses of the polyphagous spider mite herbivore Tetranychus urticae (two-spotted spider mite) revealed the presence of a set of 17 genes that code for secreted proteins belonging to the "intradiol dioxygenase-like" subgroup. Phylogenetic analyses indicate that this novel enzyme family has been acquired by horizontal gene transfer. In order to better understand the role of these proteins in T. urticae, we have structurally and functionally characterized one paralog (tetur07g02040). It was demonstrated that this protein is indeed an intradiol ring-cleavage dioxygenase, as the enzyme is able to cleave catechol between two hydroxyl-groups using atmospheric dioxygen. The enzyme was characterized functionally and structurally. The active site of the T. urticae enzyme contains an Fe cofactor that is coordinated by two histidine and two tyrosine residues, an arrangement that is similar to those observed in bacterial homologs. However, the active site is significantly more solvent exposed than in bacterial proteins. Moreover, the mite enzyme is monomeric, while almost all structurally characterized bacterial homologs form oligomeric assemblies. Tetur07g02040 is not only the first spider mite dioxygenase that has been characterized at the molecular level, but is also the first structurally characterized intradiol ring-cleavage dioxygenase originating from a eukaryote.

PubMed: 30529144
DOI: 10.1016/j.ibmb.2018.12.001

実験手法

X-RAY DIFFRACTION (2.15 Å)