The N-acyltransferase Lnt: Structure-function insights from recent simultaneous studies

Int J Biol Macromol. 2018 Oct 1:117:870-877. doi: 10.1016/j.ijbiomac.2018.05.229. Epub 2018 May 31.

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.

Keywords: Acyltransferase; Lipoproteins; Nitrilase.

Publication types

  • Review

MeSH terms

  • Acyltransferases / chemistry*
  • Acyltransferases / metabolism*
  • Bacteria / metabolism
  • Catalytic Domain
  • Crystallography, X-Ray
  • Lipoproteins / metabolism

Substances

  • Lipoproteins
  • Acyltransferases