Document Type
Article
Rights
Available under a Creative Commons Attribution Non-Commercial Share Alike 4.0 International Licence
Disciplines
Health care sciences and services, Nutrition, Dietetics, Public and environmental health
Abstract
Bacterial lipoproteins have been researched for decades due to their roles in a large number of biological functions. There were no structures of their main three membrane processing enzymes, until 2016 for Lgt and LspA, and then 2017 for Lnt with not one but three simultaneous, independent publications. We have analyzed the recent findings for this apolipoprotein N-acyltransferase Lnt, with comparisons between the novel structures, and with soluble nitrilases, to determine the significance of unique features in terms of substrate's recognition and binding mechanism influenced by exclusive residues, two transmembrane helices, and a flexible loop.
DOI
https://doi.org/10.1016/j.ijbiomac.2018.05.229
Recommended Citation
Wei Cheng, Declan A. Doyle, Toufic El Arnaout, The N-acyltransferase Lnt: Structure-function insights from recent simultaneous studies, International Journal of Biological Macromolecules, Volume 117, 2018, Pages 870-877, ISSN 0141-8130, DOI: 10.1016/j.ijbiomac.2018.05.229.
Publication Details
International Journal of Biological Macromolecules