4UR2
Crystal structure of the PCE reductive dehalogenase from S. multivorans in complex with iodide
4UR2 の概要
エントリーDOI | 10.2210/pdb4ur2/pdb |
関連するPDBエントリー | 4UQU 4UR0 4UR1 4UR3 |
分子名称 | TETRACHLOROETHENE REDUCTIVE DEHALOGENASE CATALYTIC SUBUNIT PCEA, IRON/SULFUR CLUSTER, NORPSEUDO-B12, ... (6 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 | 110386.47 |
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 Cited by 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: 25278505DOI: 10.1126/SCIENCE.1258118 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.096 Å) |
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