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.

Bibliographic Details
Main Authors: Sylvie Manuse, Nicolas L. Jean, Mégane Guinot, Jean-Pierre Lavergne, Cédric Laguri, Catherine M. Bougault, Michael S. VanNieuwenhze, Christophe Grangeasse, Jean-Pierre Simorre
Format: Article
Language:English
Published: Nature Portfolio 2016-06-01
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.
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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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