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  Dissecting the conformational complexity and mechanism of a bacterial heme transporter

Wu, D., Mehdipour, A. R., Finke, F., Goojani, H. G., Groh, R. R., Grund, T. N., et al. (2023). Dissecting the conformational complexity and mechanism of a bacterial heme transporter. Nature Chemical Biology, 19(8), 992-1003. doi:10.1038/s41589-023-01314-5.

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 Urheber:
Wu, Di1, Autor                 
Mehdipour, Ahmad Reza2, 3, Autor                 
Finke, Franziska1, Autor                 
Goojani, Hojjat G.4, Autor
Groh, Roan René1, Autor           
Grund, Tamara Natascha1, Autor                 
Reichhart, Thomas M. B.1, Autor                 
Zimmermann, Rita1, Autor           
Welsch, Sonja5, Autor                 
Bald, Dirk4, Autor
Shepherd, Mark6, Autor
Hummer, Gerhard2, 7, Autor                 
Safarian, Schara1, 8, 9, Autor                 
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
3Center for Molecular Modeling (CMM), Ghent University, Zwijnaarde, Belgium, ou_persistent22              
4Amsterdam Institute for Life and Environment (A-LIFE), AIMMS, Faculty of Science, Vrije University of Amsterdam, Amsterdam, the Netherlands, ou_persistent22              
5Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Max Planck Society, ou_3249263              
6School of Biosciences, RAPID Group, University of Kent, Canterbury, UK, ou_persistent22              
7Institute of Biophysics, Goethe University Frankfurt, Frankfurt/Main, Germany, ou_persistent22              
8Department of Microbiology and Immunology, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand, ou_persistent22              
9Fraunhofer Institute for Translational Medicine and Pharmacology ITMP, Frankfurt/Main, Germany, ou_persistent22              

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Schlagwörter: Bacteria, Computational chemistry, Structural biology, Transporters
 Zusammenfassung: Iron-bound cyclic tetrapyrroles (hemes) are redox-active cofactors in bioenergetic enzymes. However, the mechanisms of heme transport and insertion into respiratory chain complexes remain unclear. Here, we used cellular, biochemical, structural and computational methods to characterize the structure and function of the heterodimeric bacterial ABC transporter CydDC. We provide multi-level evidence that CydDC is a heme transporter required for functional maturation of cytochrome bd, a pharmaceutically relevant drug target. Our systematic single-particle cryogenic-electron microscopy approach combined with atomistic molecular dynamics simulations provides detailed insight into the conformational landscape of CydDC during substrate binding and occlusion. Our simulations reveal that heme binds laterally from the membrane space to the transmembrane region of CydDC, enabled by a highly asymmetrical inward-facing CydDC conformation. During the binding process, heme propionates interact with positively charged residues on the surface and later in the substrate-binding pocket of the transporter, causing the heme orientation to rotate 180°.

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Sprache(n): eng - English
 Datum: 2022-09-192023-03-142023-04-242023-08
 Publikationsstatus: Erschienen
 Seiten: 12
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1038/s41589-023-01314-5
BibTex Citekey: wu_dissecting_2023
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Titel: Nature Chemical Biology
  Andere : Nat. Chem. Biol.
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: New York, NY : Nature Pub. Group
Seiten: - Band / Heft: 19 (8) Artikelnummer: - Start- / Endseite: 992 - 1003 Identifikator: ISSN: 1552-4450
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000021290_1