1. Structural and molecular determinants for the interaction of ExbB from Serratia marcescens and HasB, a TonB paralog
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Valérie Biou, Ricardo Jorge Diogo Adaixo, Mohamed Chami, Pierre-Damien Coureux, Benoist Laurent, Véronique Yvette Ntsogo Enguéné, Gisele Cardoso de Amorim, Nadia Izadi-Pruneyre, Christian Malosse, Julia Chamot-Rooke, Henning Stahlberg, Philippe Delepelaire, Laboratoire de biologie physico-chimique des protéines membranaires (LBPC-PM (UMR_7099)), Institut de biologie physico-chimique (IBPC (FR_550)), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Center for Cellular Imaging and Nanoanalytics, University of Basel (Unibas), Laboratoire de Biologie Structurale de la Cellule (BIOC), École polytechnique (X)-Centre National de la Recherche Scientifique (CNRS), University of Cambridge [UK] (CAM), Bioinformatique structurale - Structural Bioinformatics, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Centre de Bioinformatique, Biostatistique et Biologie Intégrative (C3BI), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Universidade Federal do Rio de Janeiro (UFRJ), Spectrométrie de Masse pour la Biologie – Mass Spectrometry for Biology (UTechS MSBio), Institut Pasteur [Paris] (IP)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), This work was supported by grants from the ANR (HEMESTOCKEXCHANGE ANR-12-BSV3-0022-01 and LABEX DYNAMO ANR-11-LABEX-0011-01)., ANR-12-BSV3-0022,HEMESTOCKEXCHANGE,Hème et porphyrine chez des bactéries modèle: des fonctions aux mécanismes(2012), ANR-11-LABX-0011,DYNAMO,Dynamique des membranes transductrices d'énergie : biogénèse et organisation supramoléculaire.(2011), Biou, Valérie [0000-0003-1600-6717], Coureux, Pierre-Damien [0000-0002-1328-7229], Enguéné, Véronique Yvette Ntsogo [0000-0003-0096-3192], de Amorim, Gisele Cardoso [0000-0003-4348-9515], Izadi-Pruneyre, Nadia [0000-0002-6864-2961], Chamot-Rooke, Julia [0000-0002-9427-543X], Delepelaire, Philippe [0000-0002-5190-7118], and Apollo - University of Cambridge Repository
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[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM] ,MESH: Escherichia coli ,101 ,Escherichia coli Proteins ,101/28 ,101/6 ,article ,Medicine (miscellaneous) ,MESH: Escherichia coli Proteins ,Heme ,[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology ,General Biochemistry, Genetics and Molecular Biology ,631/45/535/1258/1259 ,82/80 ,MESH: Serratia marcescens ,MESH: Heme ,Escherichia coli ,MESH: Protein Binding ,631/326/41/2536 ,General Agricultural and Biological Sciences ,82/83 ,Serratia marcescens ,Protein Binding - Abstract
Funder: LABEX DYNAMO ANR-11-LABEX-0011-01, Funder: ANR HEMESTOCKEXCHANGE ANR-12-BSV3-0022-01, Funder: ANR HEMESTOCKEXCHANGE ANR-12-BSV3-0022-01 ANR LABEX DYNAMO ANR-11-LABEX-0011-01, 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.
- Published
- 2022
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