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Sökning: WFRF:(Hu Christina) > (2020-2023) > Structure and ion-r...

Structure and ion-release mechanism of P IB-4-type ATPases

Grønberg, Christina (författare)
Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark
Hu, Qiaoxia (författare)
Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark
Mahato, Dhani Ram (författare)
Umeå universitet,Umeå University,Kemiska institutionen
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Longhin, Elena (författare)
Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark
Salustros, Nina (författare)
Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark
Duelli, Annette (författare)
Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark
Lyu, Pin (författare)
Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark
Bågenholm, Viktoria (författare)
Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark
Eriksson, Jonas (författare)
Umeå universitet,Umeå University,Kemiska institutionen
Umashankar Rao, Komal (författare)
Lund University,Lunds universitet,Medicinsk mikrobiologi,Forskargrupper vid Lunds universitet,Medical Microbiology,Lund University Research Groups,Department of Laboratory Medicine, Lund University, Klinikgatan 28, Lund, Sweden
Henderson, Domhnall Iain (författare)
Department of Laboratory Medicine, Lund University, Klinikgatan 28, Lund, Sweden
Meloni, Gabriele (författare)
Department of Chemistry and Biochemistry, The University of Texas at Dallas, 800 W Campbell Rd., TX, Richardson, United States
Andersson, Magnus (författare)
Umeå universitet,Umeå University,Kemiska institutionen
Croll, Tristan (författare)
Cambridge Institute for Medical Research, Department of Haematology, University of Cambridge, Keith Peters Building, Hills Rd, Cambridge, United Kingdom
Godaly, Gabriela (författare)
Lund University,Lunds universitet,Avdelningen för mikrobiologi, immunologi och glykobiologi - MIG,Institutionen för laboratoriemedicin,Medicinska fakulteten,Medicinsk mikrobiologi,Forskargrupper vid Lunds universitet,Division of Microbiology, Immunology and Glycobiology - MIG,Department of Laboratory Medicine,Faculty of Medicine,Medical Microbiology,Lund University Research Groups,Department of Laboratory Medicine, Lund University, Klinikgatan 28, Lund, Sweden
Wang, Kaituo (författare)
Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark
Gourdon, Pontus (författare)
Lund University,Lunds universitet,Institutionen för experimentell medicinsk vetenskap,Medicinska fakulteten,Department of Experimental Medical Science,Faculty of Medicine,Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark; Department of Experimental Medical Science, Lund University, Sölvegatan 19, Lund, Sweden
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 (creator_code:org_t)
eLife Sciences Publications Ltd, 2022
2022
Engelska 21 s.
Ingår i: eLife. - : eLife Sciences Publications Ltd. - 2050-084X.
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
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  • Abstract Transition metals, such as zinc, are essential micronutrients in all organisms, but alsohighly toxic in excessive amounts. Heavy-metal transporting P-type (PIB) ATPases are crucial forhomeostasis, conferring cellular detoxification and redistribution through transport of these ionsacross cellular membranes. No structural information is available for the PIB-4-ATPases, the subclasswith the broadest cargo scope, and hence even their topology remains elusive. Here, we presentstructures and complementary functional analyses of an archetypal PIB-4-ATPase, sCoaT fromSulfitobacter sp. NAS14-1. The data disclose the architecture, devoid of classical so-called heavy-metal-binding domains (HMBDs), and provide fundamentally new insights into the mechanism anddiversity of heavy-metal transporters. We reveal several novel P-type ATPase features, includinga dual role in heavy-metal release and as an internal counter ion of an invariant histidine. We alsoestablish that the turnover of PIB-ATPases is potassium independent, contrasting to many otherP-type ATPases. Combined with new inhibitory compounds, our results open up for efforts in forexample drug discovery, since PIB-4-ATPases function as virulence factors in many pathogens.

Ämnesord

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
NATURVETENSKAP  -- Biologi -- Biofysik (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biophysics (hsv//eng)

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