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Essential Mycoplasma Glycolipid Synthase Adheres to the Cell Membrane by Means of an Amphipathic Helix
Because of the lack of cell wall, Micoplasma species require a fine control of membrane fluidity and integrity. mg517 is an essential gene of Mycoplasma genitalium responsible for the biosynthesis of membrane glycoglycerolipids. It encodes for a unique glycosyltransferase (MG517) with processive act...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6506492/ https://www.ncbi.nlm.nih.gov/pubmed/31068620 http://dx.doi.org/10.1038/s41598-019-42970-9 |
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author | Romero-García, Javier Biarnés, Xevi Planas, Antoni |
author_facet | Romero-García, Javier Biarnés, Xevi Planas, Antoni |
author_sort | Romero-García, Javier |
collection | PubMed |
description | Because of the lack of cell wall, Micoplasma species require a fine control of membrane fluidity and integrity. mg517 is an essential gene of Mycoplasma genitalium responsible for the biosynthesis of membrane glycoglycerolipids. It encodes for a unique glycosyltransferase (MG517) with processive activity, transferring activated glycosyl donors to either nude diacylglycerol or already glycosylated diacylglycerol. This dual activity, asserted to different enzymes in other species, is sensitive to and regulated by the presence of anionic lipid vesicles in vitro. We present here a computational model of the C-terminus domain of MG517 that complements a previous structural model of the N-terminus domain. By means of sequence analysis, molecular dynamics and metadynamics simulations, we have identified a short α-helix at the apical C-terminus of MG517 with clear amphipathic character. Binding to a membrane model is thermodynamically favored which suggests that this structural element guides the adhesion of MG517 to the cell membrane. We have experimentally verified that truncation of part of this helix causes a substantial reduction of glycoglycerolipids synthesis. The model proposes that MG517 recognizes and binds the diacylglycerol substrate embedded in the membrane by means of this α-helix at the C-terminus together with a previously identified binding pocket at the N-terminus. |
format | Online Article Text |
id | pubmed-6506492 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-65064922019-05-21 Essential Mycoplasma Glycolipid Synthase Adheres to the Cell Membrane by Means of an Amphipathic Helix Romero-García, Javier Biarnés, Xevi Planas, Antoni Sci Rep Article Because of the lack of cell wall, Micoplasma species require a fine control of membrane fluidity and integrity. mg517 is an essential gene of Mycoplasma genitalium responsible for the biosynthesis of membrane glycoglycerolipids. It encodes for a unique glycosyltransferase (MG517) with processive activity, transferring activated glycosyl donors to either nude diacylglycerol or already glycosylated diacylglycerol. This dual activity, asserted to different enzymes in other species, is sensitive to and regulated by the presence of anionic lipid vesicles in vitro. We present here a computational model of the C-terminus domain of MG517 that complements a previous structural model of the N-terminus domain. By means of sequence analysis, molecular dynamics and metadynamics simulations, we have identified a short α-helix at the apical C-terminus of MG517 with clear amphipathic character. Binding to a membrane model is thermodynamically favored which suggests that this structural element guides the adhesion of MG517 to the cell membrane. We have experimentally verified that truncation of part of this helix causes a substantial reduction of glycoglycerolipids synthesis. The model proposes that MG517 recognizes and binds the diacylglycerol substrate embedded in the membrane by means of this α-helix at the C-terminus together with a previously identified binding pocket at the N-terminus. Nature Publishing Group UK 2019-05-08 /pmc/articles/PMC6506492/ /pubmed/31068620 http://dx.doi.org/10.1038/s41598-019-42970-9 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Romero-García, Javier Biarnés, Xevi Planas, Antoni Essential Mycoplasma Glycolipid Synthase Adheres to the Cell Membrane by Means of an Amphipathic Helix |
title | Essential Mycoplasma Glycolipid Synthase Adheres to the Cell Membrane by Means of an Amphipathic Helix |
title_full | Essential Mycoplasma Glycolipid Synthase Adheres to the Cell Membrane by Means of an Amphipathic Helix |
title_fullStr | Essential Mycoplasma Glycolipid Synthase Adheres to the Cell Membrane by Means of an Amphipathic Helix |
title_full_unstemmed | Essential Mycoplasma Glycolipid Synthase Adheres to the Cell Membrane by Means of an Amphipathic Helix |
title_short | Essential Mycoplasma Glycolipid Synthase Adheres to the Cell Membrane by Means of an Amphipathic Helix |
title_sort | essential mycoplasma glycolipid synthase adheres to the cell membrane by means of an amphipathic helix |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6506492/ https://www.ncbi.nlm.nih.gov/pubmed/31068620 http://dx.doi.org/10.1038/s41598-019-42970-9 |
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