6R1L

Crystal structure of LmrR with bound copper phenanthroline

Summary for 6R1L

• Entry DOI: 10.2210/pdb6r1l/pdb
• Descriptor: Transcriptional regulator, PadR-like family, 1,10-PHENANTHROLINE, COPPER (II) ION, ... (4 entities in total)
• Functional Keywords: padr family, transcriptional regulator, artificial metalloenzyme, phenanthroline, dna binding protein
• Biological source: Lactococcus lactis subsp. cremoris MG1363
• Total number of polymer chains: 1
• Total formula weight: 15008.54

Authors

Reddem, R.,Thunnissen, A.M.W.H. (deposition date: 2019-03-14, release date: 2020-04-01, Last modification date: 2024-01-24)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.095 Å)