Structural basis of bidirectional allostery across the heme in a cytochrome P450 enzyme.
allosteric regulation
conformational change
cytochrome P450
ligand binding
nuclear magnetic resonance (NMR)
protein cross-linking
spectroscopy
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
08 2023
08 2023
Historique:
received:
06
03
2023
revised:
02
06
2023
accepted:
22
06
2023
medline:
31
8
2023
pubmed:
1
7
2023
entrez:
30
6
2023
Statut:
ppublish
Résumé
Cytochromes P450 (CYPs) are heme-containing enzymes that are present in all kingdoms of life and share a structurally homologous, globular protein fold. CYPs utilize structures distal to the heme to recognize and coordinate substrates, while the necessary interactions with redox partner proteins are mediated at the opposite, proximal surface. In the current study, we investigated the functional allostery across the heme for the bacterial enzyme CYP121A1, which utilizes a non-polar distal-to-distal dimer interface for specific binding of its dicyclotyrosine substrate. Fluorine-detected Nuclear Magnetic Resonance (
Identifiants
pubmed: 37390989
pii: S0021-9258(23)02005-7
doi: 10.1016/j.jbc.2023.104977
pmc: PMC10416055
pii:
doi:
Substances chimiques
Cytochrome P-450 Enzyme System
9035-51-2
Fluorine
284SYP0193
Heme
42VZT0U6YR
cytochrome P-450 CYP121
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
104977Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM133375
Pays : United States
Informations de copyright
Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that there are no conflicts of interest with the contents of this article.