6FUU
Transcriptional regulator LmrR with bound heme
Summary for 6FUU
| Entry DOI | 10.2210/pdb6fuu/pdb |
| Descriptor | Transcriptional regulator PadR family, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | artificial enzyme, complex, heme-based catalysis, transcriptional regulator, multi-drug resistance, dna binding protein |
| Biological source | Lactococcus lactis subsp. cremoris (Streptococcus cremoris) |
| Total number of polymer chains | 1 |
| Total formula weight | 15381.28 |
| Authors | Reddem, E.R.,Thunnissen, A.M.W.H. (deposition date: 2018-02-27, release date: 2018-05-16, Last modification date: 2024-01-17) |
| Primary citation | Villarino, L.,Splan, K.E.,Reddem, E.,Alonso-Cotchico, L.,Gutierrez de Souza, C.,Lledos, A.,Marechal, J.D.,Thunnissen, A.W.H.,Roelfes, G. An Artificial Heme Enzyme for Cyclopropanation Reactions. Angew. Chem. Int. Ed. Engl., 57:7785-7789, 2018 Cited by PubMed Abstract: An artificial heme enzyme was created through self-assembly from hemin and the lactococcal multidrug resistance regulator (LmrR). The crystal structure shows the heme bound inside the hydrophobic pore of the protein, where it appears inaccessible for substrates. However, good catalytic activity and moderate enantioselectivity was observed in an abiological cyclopropanation reaction. We propose that the dynamic nature of the structure of the LmrR protein is key to the observed activity. This was supported by molecular dynamics simulations, which showed transient formation of opened conformations that allow the binding of substrates and the formation of pre-catalytic structures. PubMed: 29719099DOI: 10.1002/anie.201802946 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
Download full validation report
