Structure–function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ
Placement of the bacterial division site is crucial for the creation of identical daughter cells. Here, the authors solve the structure of the MapZ protein, which helps to position the cell division protein FtsZ at the cell centre, and further analyse the function of the protein in vivo.
Main Authors: | , , , , , , , , |
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Format: | Article |
Language: | English |
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Nature Portfolio
2016-06-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/ncomms12071 |
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author | Sylvie Manuse Nicolas L. Jean Mégane Guinot Jean-Pierre Lavergne Cédric Laguri Catherine M. Bougault Michael S. VanNieuwenhze Christophe Grangeasse Jean-Pierre Simorre |
author_facet | Sylvie Manuse Nicolas L. Jean Mégane Guinot Jean-Pierre Lavergne Cédric Laguri Catherine M. Bougault Michael S. VanNieuwenhze Christophe Grangeasse Jean-Pierre Simorre |
author_sort | Sylvie Manuse |
collection | DOAJ |
description | Placement of the bacterial division site is crucial for the creation of identical daughter cells. Here, the authors solve the structure of the MapZ protein, which helps to position the cell division protein FtsZ at the cell centre, and further analyse the function of the protein in vivo. |
first_indexed | 2024-12-21T09:06:50Z |
format | Article |
id | doaj.art-139378a58a2d44e8807417c1e4afe0c4 |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-21T09:06:50Z |
publishDate | 2016-06-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-139378a58a2d44e8807417c1e4afe0c42022-12-21T19:09:19ZengNature PortfolioNature Communications2041-17232016-06-017111310.1038/ncomms12071Structure–function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZSylvie Manuse0Nicolas L. Jean1Mégane Guinot2Jean-Pierre Lavergne3Cédric Laguri4Catherine M. Bougault5Michael S. VanNieuwenhze6Christophe Grangeasse7Jean-Pierre Simorre8CNRS, Molecular Microbiology and Structural BiochemistryUniversité Grenoble Alpes, Institut de Biologie StructuraleCNRS, Molecular Microbiology and Structural BiochemistryCNRS, Molecular Microbiology and Structural BiochemistryUniversité Grenoble Alpes, Institut de Biologie StructuraleUniversité Grenoble Alpes, Institut de Biologie StructuraleDepartment of Chemistry, Indiana UniversityCNRS, Molecular Microbiology and Structural BiochemistryUniversité Grenoble Alpes, Institut de Biologie StructuralePlacement of the bacterial division site is crucial for the creation of identical daughter cells. Here, the authors solve the structure of the MapZ protein, which helps to position the cell division protein FtsZ at the cell centre, and further analyse the function of the protein in vivo.https://doi.org/10.1038/ncomms12071 |
spellingShingle | Sylvie Manuse Nicolas L. Jean Mégane Guinot Jean-Pierre Lavergne Cédric Laguri Catherine M. Bougault Michael S. VanNieuwenhze Christophe Grangeasse Jean-Pierre Simorre Structure–function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ Nature Communications |
title | Structure–function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ |
title_full | Structure–function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ |
title_fullStr | Structure–function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ |
title_full_unstemmed | Structure–function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ |
title_short | Structure–function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ |
title_sort | structure function analysis of the extracellular domain of the pneumococcal cell division site positioning protein mapz |
url | https://doi.org/10.1038/ncomms12071 |
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