7ZCL

Unspecific peroxygenase from Collariella virescens

7ZCL の概要

• エントリーDOI: 10.2210/pdb7zcl/pdb
• 分子名称: Collariella virescens UPO, HEME C, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: unspecific peroxygenases (upo), collariella virescens, short upo family, molecular structure, fatty acid epoxidation, oxidoreductase
• 由来する生物種: Collariella virescens; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53203.76

構造登録者

Santillana, E.,Romero, A. (登録日: 2022-03-28, 公開日: 2022-05-18, 最終更新日: 2024-01-31)

主引用文献

Linde, D.,Santillana, E.,Fernandez-Fueyo, E.,Gonzalez-Benjumea, A.,Carro, J.,Gutierrez, A.,Martinez, A.T.,Romero, A.
Structural Characterization of Two Short Unspecific Peroxygenases: Two Different Dimeric Arrangements.
Antioxidants, 11:-, 2022

PubMed Abstract: Unspecific peroxygenases (UPOs) are extracellular fungal enzymes of biotechnological interest as self-sufficient (and more stable) counterparts of cytochrome P450 monooxygenases, the latter being present in most living cells. Expression hosts and structural information are crucial for exploiting UPO diversity (over eight thousand UPO-type genes were identified in sequenced genomes) in target reactions of industrial interest. However, while many thousands of entries in the Protein Data Bank include molecular coordinates of P450 enzymes, only 19 entries correspond to UPO enzymes, and UPO structures from only two species ( and sp.) have been published to date. In the present study, two UPOs from the basidiomycete (rUPO) and the ascomycete (rUPO) were crystallized after sequence optimization and expression as active soluble enzymes. Crystals of rUPO and rUPO were obtained at sufficiently high resolution (1.45 and 1.95 Å, respectively) and the corresponding structures were solved by molecular replacement. The crystal structures of the two enzymes (and two mutated variants) showed dimeric proteins. Complementary biophysical and molecular biology studies unveiled the diverse structural bases of the dimeric nature of the two enzymes. Intermolecular disulfide bridge and parallel association between two α-helices, among other interactions, were identified at the dimer interfaces. Interestingly, one of the rUPO variants incorporated the ability to produce fatty acid diepoxides-reactive compounds with valuable cross-linking capabilities-due to removal of the enzyme C-terminal tail located near the entrance of the heme access channel. In conclusion, different dimeric arrangements could be described in (short) UPO crystal structures.

PubMed: 35624755
DOI: 10.3390/antiox11050891

実験手法

X-RAY DIFFRACTION (1.95 Å)