A novel fold for acyltransferase-3 (AT3) proteins provides a framework for transmembrane acyl-group transfer.

ABSTRACT: Acylation of diverse carbohydrates occurs across all domains of life and can be catalysed by proteins with a membrane bound acyltransferase-3 (AT3) domain (PF01757). In bacteria, these proteins are essential in processes including symbiosis, resistance to viruses and antimicrobials, and biosynthesis of antibiotics, yet their structure and mechanism are largely unknown. In this study, evolutionary co-variance analysis was used to build a computational model of the structure of a bacterial O-antigen modifying acetyltransferase, OafB. The resulting structure exhibited a novel fold for the AT3 domain, which molecular dynamics simulations demonstrated is stable in the membrane. The AT3 domain contains 10 transmembrane helices arranged to form a large cytoplasmic cavity lined by residues known t

SUBMITTER: Newman KE 

PROVIDER: S-EPMC9833829 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature