1. Structural modeling of a novel membrane-bound globin-coupled sensor in Geobacter sulfurreducens
- Author
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Claudio D. Schuster, David Hoogewijs, Sabine Van Doorslaer, Salvador I. Drusin, Luc Moens, Sylvia Dewilde, Catherine Vénien-Bryan, Marcelo A. Martí, Frank Sobott, Dietmar Hammerschmid, Charline Fagnen, Francesca Germani, Institut de minéralogie, de physique des matériaux et de cosmochimie (IMPMC), Muséum national d'Histoire naturelle (MNHN)-Institut de recherche pour le développement [IRD] : UR206-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de biologie et pharmacologie appliquée (LBPA), Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Ecole Normale Supérieure Paris-Saclay (ENS Paris Saclay), Université de Fribourg = University of Fribourg (UNIFR), Universidad de Buenos Aires [Buenos Aires] (UBA), Biomedical Sciences, University of Antwerp (UA), University of Antwerp, Department of Physics, and University of Leeds
- Subjects
DPV, differential pulse voltammetry ,PDE, phosphodiesterase ,Transmembrane-coupled globins ,[SDV]Life Sciences [q-bio] ,SaktrHb, Streptomyces avermitilis truncated hemoglobin-antibiotic monooxygenase ,Biochemistry ,Transmembrane domain ,TmD, Transmembrane domain ,chemistry.chemical_compound ,0302 clinical medicine ,Structural Biology ,Globin-coupled sensor ,RR, resonance Raman ,TD, Transmitter domain ,IM-MS, ion mobility-mass spectrometry ,GsGCS162, GD of GsGCS ,Geobacter sulfurreducens ,Heme ,0303 health sciences ,CeGLB26, Caenorhabditis elegans globin 26 ,biology ,Gb, globin ,CIU, collision-induced unfolding ,CMC, critical micelle concentration ,PccGCS, Pectobacterium carotivorum GCS ,CV, cyclic voltammetry ,Transmembrane protein ,Computer Science Applications ,Chemistry ,GD, globin domain ,030220 oncology & carcinogenesis ,MtTrHbO, Mycobacterium tuberculosis truncated hemoglobin O ,Signal transduction ,Engineering sciences. Technology ,Research Article ,PcMb, Physether catodon myoglobin ,Biotechnology ,AfGcHK, Anaeromyxobacter sp. Fw109-5 GcHK ,BsHemAT, Bacillus subtilis HemAT ,NH4OAc, ammonium acetate ,LmHemAC, Leishmania major HemAC ,CeGLB6, Caenorhabditis elegans globin 6 ,Biophysics ,GGDEF, Gly-Gly-Asp-Glu-Phe motive ,GCS, globin-coupled sensor ,AsFRMF, Ascaris suum FRMF-amide receptor ,SwMb, myoglobin from sperm whale ,GintHb, hemoglobin from Gasterophilus intestinalis ,03 medical and health sciences ,Tetramer ,Genetics ,SHE, standard hydrogen electrode ,BpGReg, Bordetella pertussis Greg ,GsGCS, Geobacter sulfurreducens GCS ,AvGReg, Azotobacter vinilandii Greg ,Globin ,MaPgb, Methanosarcina acetivorans protoglobin ,Biology ,ComputingMethodologies_COMPUTERGRAPHICS ,CeGLB33, Caenorhabditis elegans globin 33 ,030304 developmental biology ,EcDosC, Escherichia coli Dos with DGC activity ,OG, n-octyl-β-d-glucopyranoside ,DDM, n-dodecyl-β-d-maltoside ,biology.organism_classification ,FMRF, H-Phe-Met-Arg-Phe-NH2 neuropeptide ,PsiE, phosphate-starvation-inducible E ,SCE, saturated calomel electrode ,chemistry ,mNgb, mouse neuroglobin ,CCS, collision cross section ,Linker ,TP248.13-248.65 - Abstract
Graphical abstract, Globin-coupled sensors (GCS) usually consist of three domains: a sensor/globin, a linker, and a transmitter domain. The globin domain (GD), activated by ligand binding and/or redox change, induces an intramolecular signal transduction resulting in a response of the transmitter domain. Depending on the nature of the transmitter domain, GCSs can have different activities and functions, including adenylate and di-guanylate cyclase, histidine kinase activity, aerotaxis and/or oxygen sensing function. The gram-negative delta-proteobacterium Geobacter sulfurreducens expresses a protein with a GD covalently linked to a four transmembrane domain, classified, by sequence similarity, as GCS (GsGCS). While its GD is fully characterized, not so its transmembrane domain, which is rarely found in the globin superfamily. In the present work, GsGCS was characterized spectroscopically and by native ion mobility-mass spectrometry in combination with cryo-electron microscopy. Although lacking high resolution, the oligomeric state and the electron density map were valuable for further rational modeling of the full-length GsGCS structure. This model demonstrates that GsGCS forms a transmembrane domain-driven tetramer with minimal contact between the GDs and with the heme groups oriented outward. This organization makes an intramolecular signal transduction less likely. Our results, including the auto-oxidation rate and redox potential, suggest a potential role for GsGCS as redox sensor or in a membrane-bound e−/H+ transfer. As such, GsGCS might act as a player in connecting energy production to the oxidation of organic compounds and metal reduction. Database searches indicate that GDs linked to a four or seven helices transmembrane domain occur more frequently than expected.
- Published
- 2021