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- Title
Structural and molecular determinants for the interaction of ExbB from Serratia marcescens and HasB, a TonB paralog.
- Authors
Biou, Valérie; Adaixo, Ricardo Jorge Diogo; Chami, Mohamed; Coureux, Pierre-Damien; Laurent, Benoist; Enguéné, Véronique Yvette Ntsogo; de Amorim, Gisele Cardoso; Izadi-Pruneyre, Nadia; Malosse, Christian; Chamot-Rooke, Julia; Stahlberg, Henning; Delepelaire, Philippe
- Abstract
ExbB and ExbD are cytoplasmic membrane proteins that associate with TonB to convey the energy of the proton-motive force to outer membrane receptors in Gram-negative bacteria for iron uptake. The opportunistic pathogen Serratia marcescens (Sm) possesses both TonB and a heme-specific TonB paralog, HasB. ExbBSm has a long periplasmic extension absent in other bacteria such as E. coli (Ec). Long ExbB's are found in several genera of Alphaproteobacteria, most often in correlation with a hasB gene. We investigated specificity determinants of ExbBSm and HasB. We determined the cryo-EM structures of ExbBSm and of the ExbB-ExbDSm complex from S. marcescens. ExbBSm alone is a stable pentamer, and its complex includes two ExbD monomers. We showed that ExbBSm extension interacts with HasB and is involved in heme acquisition and we identified key residues in the membrane domain of ExbBSm and ExbBEc, essential for function and likely involved in the interaction with TonB/HasB. Our results shed light on the class of inner membrane energy machinery formed by ExbB, ExbD and HasB. Cryo-EM structures of the ExbB and ExbB-ExbD membrane protein complexes in the Gram-negative bacteria Serratia marcescens reveal insights into inner membrane machinery and interactions specific to the Has system.
- Subjects
SERRATIA marcescens; MOLECULAR interactions; ESCHERICHIA coli; FORCE &; energy; MEMBRANE proteins
- Publication
Communications Biology, 2022, Vol 5, Issue 1, p1
- ISSN
2399-3642
- Publication type
Article
- DOI
10.1038/s42003-022-03306-y