Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis
Lipoproteins are essential components of bacterial membranes. Here the authors present the crystal structures ofPseudomonas aeruginosa and Escherichia coliapolipoprotein N-acyltransferase, which catalyses the final step in the lipoprotein synthesis pathway, and give insights into its mechanism.
Main Authors: | , , , , , , , , , , , |
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Format: | Article |
Language: | English |
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Nature Portfolio
2017-07-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/ncomms15952 |
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author | Maciej Wiktor Dietmar Weichert Nicole Howe Chia-Ying Huang Vincent Olieric Coilín Boland Jonathan Bailey Lutz Vogeley Phillip J. Stansfeld Nienke Buddelmeijer Meitian Wang Martin Caffrey |
author_facet | Maciej Wiktor Dietmar Weichert Nicole Howe Chia-Ying Huang Vincent Olieric Coilín Boland Jonathan Bailey Lutz Vogeley Phillip J. Stansfeld Nienke Buddelmeijer Meitian Wang Martin Caffrey |
author_sort | Maciej Wiktor |
collection | DOAJ |
description | Lipoproteins are essential components of bacterial membranes. Here the authors present the crystal structures ofPseudomonas aeruginosa and Escherichia coliapolipoprotein N-acyltransferase, which catalyses the final step in the lipoprotein synthesis pathway, and give insights into its mechanism. |
first_indexed | 2024-12-17T10:28:55Z |
format | Article |
id | doaj.art-3e70da5018ac4c64b19755f2a8e71164 |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-17T10:28:55Z |
publishDate | 2017-07-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-3e70da5018ac4c64b19755f2a8e711642022-12-21T21:52:34ZengNature PortfolioNature Communications2041-17232017-07-018111310.1038/ncomms15952Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesisMaciej Wiktor0Dietmar Weichert1Nicole Howe2Chia-Ying Huang3Vincent Olieric4Coilín Boland5Jonathan Bailey6Lutz Vogeley7Phillip J. Stansfeld8Nienke Buddelmeijer9Meitian Wang10Martin Caffrey11Membrane Structural and Functional Biology (MS&FB) Group, School of Medicine and School of Biochemistry and Immunology, Trinity College DublinMembrane Structural and Functional Biology (MS&FB) Group, School of Medicine and School of Biochemistry and Immunology, Trinity College DublinMembrane Structural and Functional Biology (MS&FB) Group, School of Medicine and School of Biochemistry and Immunology, Trinity College DublinMembrane Structural and Functional Biology (MS&FB) Group, School of Medicine and School of Biochemistry and Immunology, Trinity College DublinSwiss Light Source, Paul Scherrer InstituteMembrane Structural and Functional Biology (MS&FB) Group, School of Medicine and School of Biochemistry and Immunology, Trinity College DublinMembrane Structural and Functional Biology (MS&FB) Group, School of Medicine and School of Biochemistry and Immunology, Trinity College DublinMembrane Structural and Functional Biology (MS&FB) Group, School of Medicine and School of Biochemistry and Immunology, Trinity College DublinDepartment of Biochemistry, University of OxfordDepartment of Microbiology, Institut Pasteur, Biology and Genetics of the Bacterial Cell Wall UnitSwiss Light Source, Paul Scherrer InstituteMembrane Structural and Functional Biology (MS&FB) Group, School of Medicine and School of Biochemistry and Immunology, Trinity College DublinLipoproteins are essential components of bacterial membranes. Here the authors present the crystal structures ofPseudomonas aeruginosa and Escherichia coliapolipoprotein N-acyltransferase, which catalyses the final step in the lipoprotein synthesis pathway, and give insights into its mechanism.https://doi.org/10.1038/ncomms15952 |
spellingShingle | Maciej Wiktor Dietmar Weichert Nicole Howe Chia-Ying Huang Vincent Olieric Coilín Boland Jonathan Bailey Lutz Vogeley Phillip J. Stansfeld Nienke Buddelmeijer Meitian Wang Martin Caffrey Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis Nature Communications |
title | Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis |
title_full | Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis |
title_fullStr | Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis |
title_full_unstemmed | Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis |
title_short | Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis |
title_sort | structural insights into the mechanism of the membrane integral n acyltransferase step in bacterial lipoprotein synthesis |
url | https://doi.org/10.1038/ncomms15952 |
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