5OCS

Ene-reductase (ER/OYE) from Ralstonia (Cupriavidus) metallidurans

5OCS の概要

• エントリーDOI: 10.2210/pdb5ocs/pdb
• 分子名称: Putative NADH-depentdent flavin oxidoreductase, FLAVIN MONONUCLEOTIDE, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: old yellow enzyme, ene-reductase, flavoprotein
• 由来する生物種: Cupriavidus metallidurans
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 162181.24

構造登録者

Opperman, D.J. (登録日: 2017-07-03, 公開日: 2017-09-06, 最終更新日: 2024-01-17)

主引用文献

Opperman, D.J.
Structural investigation into the C-terminal extension of the ene-reductase from Ralstonia (Cupriavidus) metallidurans.
Proteins, 85:2252-2257, 2017

PubMed Abstract: Ene-reductases (ERs), or Old Yellow Enzymes, catalyze the asymmetric reduction of various activated alkenes. This class of biocatalysts is considered an attractive alternative to current chemical technologies for hydrogenation due to their high selectivity and specificity. Here the X-ray crystal structure of RmER, a "thermophilic"-like ER from Ralstonia (Cupriavidus) metallidurans, is reported. Unlike other members of this class of ERs, RmER is monomeric in solution which we previously related to its atypical elongated C-terminus. A typical dimer interface was however observed in our crystal structure, with the conserved Arg-"finger" forming part of the adjacent monomer's active site and the elongated C-terminus extending into the active site through contacting the "capping" domain. This dimerization also resulted in the loss of one FMN cofactor from each dimer pair. This potential transient dimerization and dissociation of FMN could conceivably explain the rapid rates previously observed when an FMN light-driven cofactor regeneration system was used during catalysis with RmER.

PubMed: 28833623
DOI: 10.1002/prot.25372

実験手法

X-RAY DIFFRACTION (1.7 Å)