6R1L

Crystal structure of LmrR with bound copper phenanthroline

6R1L の概要

• エントリーDOI: 10.2210/pdb6r1l/pdb
• 分子名称: Transcriptional regulator, PadR-like family, 1,10-PHENANTHROLINE, COPPER (II) ION, ... (4 entities in total)
• 機能のキーワード: padr family, transcriptional regulator, artificial metalloenzyme, phenanthroline, dna binding protein
• 由来する生物種: Lactococcus lactis subsp. cremoris MG1363
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15008.54

構造登録者

Reddem, R.,Thunnissen, A.M.W.H. (登録日: 2019-03-14, 公開日: 2020-04-01, 最終更新日: 2024-01-24)

主引用文献

Villarino, L.,Chordia, S.,Alonso-Cotchico, L.,Reddem, E.,Zhou, Z.,Thunnissen, A.M.W.H.,Marechal, J.D.,Roelfes, G.
Cofactor Binding Dynamics Influence the Catalytic Activity and Selectivity of an Artificial Metalloenzyme.
Acs Catalysis, 10:11783-11790, 2020

PubMed Abstract: We present an artificial metalloenzyme based on the transcriptional regulator LmrR that exhibits dynamics involving the positioning of its abiological metal cofactor. The position of the cofactor, in turn, was found to be related to the preferred catalytic reactivity, which is either the enantioselective Friedel-Crafts alkylation of indoles with β-substituted enones or the tandem Friedel-Crafts alkylation/enantioselective protonation of indoles with α-substituted enones. The artificial metalloenzyme could be specialized for one of these catalytic reactions introducing a single mutation in the protein. The relation between cofactor dynamics and activity and selectivity in catalysis has not been described for natural enzymes and, to date, appears to be particular for artificial metalloenzymes.

PubMed: 33101759
DOI: 10.1021/acscatal.0c01619

実験手法

X-RAY DIFFRACTION (2.095 Å)