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

Wei Cheng; Declan A. Doyle; Toufic El Arnaout

doi:10.1016/j.ijbiomac.2018.05.229

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

Wei Cheng, Declan A. Doyle, Toufic El Arnaout

Research output: Contribution to journal › Review article › peer-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.

Original language	English
Pages (from-to)	870-877
Number of pages	8
Journal	International Journal of Biological Macromolecules
Volume	117
DOIs	https://doi.org/10.1016/j.ijbiomac.2018.05.229
Publication status	Published - 1 Oct 2018

Keywords

Acyltransferase
Lipoproteins
Nitrilase

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10.1016/j.ijbiomac.2018.05.229

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title = "The N-acyltransferase Lnt: Structure-function insights from recent simultaneous studies",

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",

author = "Wei Cheng and Doyle, \{Declan A.\} and \{El Arnaout\}, Toufic",

note = "Publisher Copyright: {\textcopyright} 2018 Elsevier B.V.",

year = "2018",

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doi = "10.1016/j.ijbiomac.2018.05.229",

language = "English",

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journal = "International Journal of Biological Macromolecules",

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T1 - The N-acyltransferase Lnt

T2 - Structure-function insights from recent simultaneous studies

AU - Cheng, Wei

AU - Doyle, Declan A.

AU - El Arnaout, Toufic

PY - 2018/10/1

Y1 - 2018/10/1

N2 - 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.

AB - 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.

KW - Acyltransferase

KW - Lipoproteins

KW - Nitrilase

UR - https://www.scopus.com/pages/publications/85048520390

U2 - 10.1016/j.ijbiomac.2018.05.229

DO - 10.1016/j.ijbiomac.2018.05.229

M3 - Review article

SN - 0141-8130

VL - 117

SP - 870

EP - 877

JO - International Journal of Biological Macromolecules

JF - International Journal of Biological Macromolecules

ER -

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

Abstract

Keywords

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