Rocking the MBOAT: Structural insights into the membrane bound O-acyltransferase family.
Journal
Current opinion in structural biology
ISSN: 1879-033X
Titre abrégé: Curr Opin Struct Biol
Pays: England
ID NLM: 9107784
Informations de publication
Date de publication:
06 2023
06 2023
Historique:
received:
10
11
2022
revised:
28
02
2023
accepted:
06
03
2023
medline:
5
6
2023
pubmed:
12
4
2023
entrez:
11
4
2023
Statut:
ppublish
Résumé
The membrane-bound O-acyltransferase (MBOAT) superfamily catalyses the transfer of acyl chains to substrates implicated in essential cellular functions. Aberrant function of MBOATs is associated with various diseases and MBOATs are promising drug targets. There has been recent progress in structural characterisation of MBOATs, advancing our understanding of their functional mechanism. Integrating information across the MBOAT family, we characterise a common MBOAT fold and provide a blueprint for substrate and inhibitor engagement. This work provides context for the diverse substrates, mechanisms, and evolutionary relationships of protein and small-molecule MBOATs. Further work should aim to characterise MBOATs, as inherently lipid-associated proteins, within their membrane environment.
Identifiants
pubmed: 37040671
pii: S0959-440X(23)00063-5
doi: 10.1016/j.sbi.2023.102589
pii:
doi:
Substances chimiques
Acyltransferases
EC 2.3.-
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
102589Informations de copyright
Copyright © 2023 The Author(s). Published by Elsevier Ltd.. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.