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

  • Kahlan E. Newman (Creator)
  • Sarah N. Tindall (Department of Psychology, York Neuroimaging Centre, University of York, York, YO10 5NY, UK; Centre for Neuroscience, Hull-York Medical School, University of York, York, YO10 5DD, UK.) (Creator)
  • Sophie L. Mader (Creator)
  • Syma Khalid (Creator)
  • Gavin Hugh Thomas (Creator)
  • Marjan Van Der Woude (Creator)



In this study, evolutionary co-variance analysis was used to build an <em>in silico </em>model for the structure of the bacterial O-antigen modifying acetyltransferase protein, OafB. This model was subjected to molecular dynamics simulations to assess its stability, dynamics, and interactions with the putative acetyl donor substrate, acetyl coenzyme-A, and O-antigen acceptor substrate. Files deposited here are the trajectories (without water, every 10th frame) and run input files from the molecular dynamics simulations presented in this work. 

Preprint: https://www.biorxiv.org/content/10.1101/2022.06.30.498268

External deposit with Zenodo
Date made available30 Jun 2022

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