Modulation of the lytic apparatus by the FtsEX complex within the bacterial division machinery.

Autor: Alcorlo M; Department of Crystallography and Structural Biology, Instituto de Química-Física 'Blas Cabrera', Consejo Superior de Investigaciones Científicas, Madrid, Spain., Martínez-Caballero S; Department of Crystallography and Structural Biology, Instituto de Química-Física 'Blas Cabrera', Consejo Superior de Investigaciones Científicas, Madrid, Spain., Li J; Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore.; Department of Biological Sciences, Center for Bioimaging Sciences, National University of Singapore, Singapore., Sham LT; Infectious Diseases Translational Research Programme and Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore., Luo M; Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore.; Department of Biological Sciences, Center for Bioimaging Sciences, National University of Singapore, Singapore., Hermoso JA; Department of Crystallography and Structural Biology, Instituto de Química-Física 'Blas Cabrera', Consejo Superior de Investigaciones Científicas, Madrid, Spain.
Jazyk: angličtina
Zdroj: FEBS letters [FEBS Lett] 2024 Jun 07. Date of Electronic Publication: 2024 Jun 07.
DOI: 10.1002/1873-3468.14953
Abstrakt: The FtsEX membrane complex constitutes an essential component of the ABC transporter superfamily, widely distributed among bacterial species. It governs peptidoglycan degradation for cell division, acting as a signal transmitter rather than a substrate transporter. Through the ATPase activity of FtsE, it facilitates signal transmission from the cytosol across the membrane to the periplasm, activating associated peptidoglycan hydrolases. This review concentrates on the latest structural advancements elucidating the architecture of the FtsEX complex and its interplay with lytic enzymes or regulatory counterparts. The revealed three-dimensional structures unveil a landscape wherein a precise array of intermolecular interactions, preserved across diverse bacterial species, afford meticulous spatial and temporal control over the cell division process.
(© 2024 The Author(s). FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)
Databáze: MEDLINE
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