5WHS

Crystal structure of the catalase-peroxidase from Neurospora crassa at 2.6 A

5WHS の概要

• エントリーDOI: 10.2210/pdb5whs/pdb
• 関連するPDBエントリー: 5WHQ
• 分子名称: Catalase-peroxidase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: catalase-peroxidase, neurospora crassa, heme, hydrogen peroxide, oxidoreductase
• 由来する生物種: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
• 細胞内の位置: Cytoplasm : Q8X182
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 171655.38

構造登録者

Diaz-Vilchis, A.,Vega-Garcia, V.,Rudino-Pinera, E.,Hansberg, W. (登録日: 2017-07-18, 公開日: 2018-01-17, 最終更新日: 2023-11-15)

主引用文献

Vega-Garcia, V.,Diaz-Vilchis, A.,Saucedo-Vazquez, J.P.,Solano-Peralta, A.,Rudino-Pinera, E.,Hansberg, W.
Structure, kinetics, molecular and redox properties of a cytosolic and developmentally regulated fungal catalase-peroxidase.
Arch. Biochem. Biophys., 640:17-26, 2018

PubMed Abstract: CAT-2, a cytosolic catalase-peroxidase (CP) from Neurospora crassa, which is induced during asexual spore formation, was heterologously expressed and characterized. CAT-2 had the Met-Tyr-Trp (M-Y-W) adduct required for catalase activity. Its K for HO was micromolar for peroxidase and millimolar for catalase activity. A E = -158 mV reduction potential value was obtained and the Soret band shift suggested a mixture of low and high spin ferric iron. CAT-2 EPR spectrum at 10 K indicated an axial and a rhombic component. With peroxyacetic acid (PAA), formation of Compound I* was observed with EPR. CAT-2 homodimer crystallographic structure contained two K ions; Glu107 residues were displaced to bind them. CAT-2 showed the essential amino acid residues for activity in similar positions to other CPs. CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. A perhydroxy modification of the indole nitrogen of Trp90 was oriented toward the catalytic His91. In contrast to cytochrome c peroxidase and ascorbate peroxidase, the catalase-peroxidase heme propionates are not exposed to the solvent. Together with other N. crassa enzymes that utilize HO as a substrate, CAT-2 has many tryptophan and proline residues at its surface, probably related to HO selection in water.

PubMed: 29305053
DOI: 10.1016/j.abb.2017.12.021

実験手法

X-RAY DIFFRACTION (2.6 Å)