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

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

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.

Acyltransferase, Lipoproteins, Nitrilase
0141-8130
870-877
Cheng, Wei
3eb69813-0add-4bab-860a-0a8c9e0c1da0
Doyle, Declan A.
f85f52c8-ce43-4f15-bd06-1df106f73b26
El Arnaout, Toufic
67bba7a4-c14b-4842-9ce2-f23715536fa7
Cheng, Wei
3eb69813-0add-4bab-860a-0a8c9e0c1da0
Doyle, Declan A.
f85f52c8-ce43-4f15-bd06-1df106f73b26
El Arnaout, Toufic
67bba7a4-c14b-4842-9ce2-f23715536fa7

Cheng, Wei, Doyle, Declan A. and El Arnaout, Toufic (2018) The N-acyltransferase Lnt: structure-function insights from recent simultaneous studies. International Journal of Biological Macromolecules, 117, 870-877. (doi:10.1016/j.ijbiomac.2018.05.229).

Record type: Review

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.

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More information

Accepted/In Press date: 30 May 2018
e-pub ahead of print date: 31 May 2018
Published date: 1 October 2018
Keywords: Acyltransferase, Lipoproteins, Nitrilase

Identifiers

Local EPrints ID: 423792
URI: http://eprints.soton.ac.uk/id/eprint/423792
ISSN: 0141-8130
PURE UUID: 99e5d45a-a278-4686-814c-f09576c81b15

Catalogue record

Date deposited: 01 Oct 2018 16:31
Last modified: 26 Nov 2021 00:17

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Contributors

Author: Wei Cheng
Author: Declan A. Doyle
Author: Toufic El Arnaout

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