6C3D

O2-, PLP-dependent L-arginine hydroxylase RohP quinonoid II complex

6C3D の概要

• エントリーDOI: 10.2210/pdb6c3d/pdb
• 分子名称: Uncharacterized protein, 1,2-ETHANEDIOL, (2E,3E)-5-carbamimidamido-2-{[(Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1H)-ylidene}methyl]imino}pent-3-enoic acid, ... (5 entities in total)
• 機能のキーワード: o2-, plp-dependent hydroxylase, biosynthetic protein
• 由来する生物種: Streptomyces cattleya (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96220.94

構造登録者

Hedges, J.B.,Ryan, K.S. (登録日: 2018-01-09, 公開日: 2018-03-07, 最終更新日: 2023-10-04)

主引用文献

Hedges, J.B.,Kuatsjah, E.,Du, Y.L.,Eltis, L.D.,Ryan, K.S.
Snapshots of the Catalytic Cycle of an O2, Pyridoxal Phosphate-Dependent Hydroxylase.
ACS Chem. Biol., 13:965-974, 2018

PubMed Abstract: Enzymes that catalyze hydroxylation of unactivated carbons normally contain heme and nonheme iron cofactors. By contrast, how a pyridoxal phosphate (PLP)-dependent enzyme could catalyze such a hydroxylation was unknown. Here, we investigate RohP, a PLP-dependent enzyme that converts l-arginine to ( S)-4-hydroxy-2-ketoarginine. We determine that the RohP reaction consumes oxygen with stoichiometric release of HO. To understand this unusual chemistry, we obtain ∼1.5 Å resolution structures that capture intermediates along the catalytic cycle. Our data suggest that RohP carries out a four-electron oxidation and a stereospecific alkene hydration to give the ( S)-configured product. Together with our earlier studies on an O, PLP-dependent l-arginine oxidase, our work suggests that there is a shared pathway leading to both oxidized and hydroxylated products from l-arginine.

PubMed: 29466666
DOI: 10.1021/acschembio.8b00039

実験手法

X-RAY DIFFRACTION (1.55 Å)