Structural Characterization of the Essential Cell Division Protein FtsE and Its Interaction with FtsX in Streptococcus pneumoniae.

ABC transporters ATPase FtsEX Streptococcus pneumoniae X-ray crystallography cell division peptidoglycan hydrolases protein-protein interactions

Journal

mBio
ISSN: 2150-7511
Titre abrégé: mBio
Pays: United States
ID NLM: 101519231

Informations de publication

Date de publication:
01 09 2020
Historique:
entrez: 3 9 2020
pubmed: 3 9 2020
medline: 21 7 2021
Statut: epublish

Résumé

FtsEX is a membrane complex widely conserved across diverse bacterial genera and involved in critical processes such as recruitment of division proteins and in spatial and temporal regulation of muralytic activity during cell division or sporulation. FtsEX is a member of the ABC transporter superfamily. The component FtsX is an integral membrane protein, whereas FtsE is an ATPase and is required for the transmission of a conformational signal from the cytosol through the membrane to regulate the activity of cell wall hydrolases in the periplasm. Both proteins are essential in the major human respiratory pathogenic bacterium

Identifiants

pubmed: 32873757
pii: mBio.01488-20
doi: 10.1128/mBio.01488-20
pmc: PMC7468199
pii:
doi:

Substances chimiques

ATP-Binding Cassette Transporters 0
Bacterial Proteins 0
Cell Cycle Proteins 0
FtsX protein, bacteria 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM029764
Pays : United States

Informations de copyright

Copyright © 2020 Alcorlo et al.

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Auteurs

Martin Alcorlo (M)

Department of Crystallography and Structural Biology, Institute of Physical-Chemistry "Rocasolano", Spanish National Research Council (CSIC), Madrid, Spain.

Daniel Straume (D)

Department of Chemistry, Biotechnology, and Food Science, Norwegian University of Life Sciences, Ås, Norway.

Joe Lutkenhaus (J)

Department of Microbiology, Molecular Genetics, and Immunology, University of Kansas Medical Center, Kansas City, Kansas, USA.

Leiv Sigve Håvarstein (LS)

Department of Chemistry, Biotechnology, and Food Science, Norwegian University of Life Sciences, Ås, Norway sigve.havarstein@nmbu.no xjuan@iqfr.csic.es.

Juan A Hermoso (JA)

Department of Crystallography and Structural Biology, Institute of Physical-Chemistry "Rocasolano", Spanish National Research Council (CSIC), Madrid, Spain sigve.havarstein@nmbu.no xjuan@iqfr.csic.es.

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Classifications MeSH