4UR0

Crystal structure of the PCE reductive dehalogenase from S. multivorans in complex with trichloroethene

4UR0 の概要

• エントリーDOI: 10.2210/pdb4ur0/pdb
• 関連するPDBエントリー: 4UQU 4UR1 4UR2 4UR3
• 分子名称: TETRACHLOROETHENE REDUCTIVE DEHALOGENASE CATALYTIC SUBUNIT PCEA, IRON/SULFUR CLUSTER, NORPSEUDO-B12, ... (7 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: SULFUROSPIRILLUM MULTIVORANS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 109426.25

構造登録者

Bommer, M.,Kunze, C.,Fesseler, J.,Schubert, T.,Diekert, G.,Dobbek, H. (登録日: 2014-06-25, 公開日: 2014-10-15, 最終更新日: 2024-05-08)

主引用文献

Bommer, M.,Kunze, C.,Fesseler, J.,Schubert, T.,Diekert, G.,Dobbek, H.
Structural Basis for Organohalide Respiration.
Science, 346:455-, 2014

PubMed Abstract: Organohalide-respiring microorganisms can use a variety of persistent pollutants, including trichloroethene (TCE), as terminal electron acceptors. The final two-electron transfer step in organohalide respiration is catalyzed by reductive dehalogenases. Here we report the x-ray crystal structure of PceA, an archetypal dehalogenase from Sulfurospirillum multivorans, as well as structures of PceA in complex with TCE and product analogs. The active site harbors a deeply buried norpseudo-B12 cofactor within a nitroreductase fold, also found in a mammalian B12 chaperone. The structures of PceA reveal how a cobalamin supports a reductive haloelimination exploiting a conserved B12-binding scaffold capped by a highly variable substrate-capturing region.

PubMed: 25278505
DOI: 10.1126/SCIENCE.1258118

実験手法

X-RAY DIFFRACTION (1.798 Å)