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
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
1 October 2018
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, .
(doi:10.1016/j.ijbiomac.2018.05.229).
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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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
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Date deposited: 01 Oct 2018 16:31
Last modified: 17 Mar 2024 12:07
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Author:
Wei Cheng
Author:
Toufic El Arnaout
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