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Structure and ion-r...
Structure and ion-release mechanism of P IB-4-type ATPases
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- Grønberg, Christina (author)
- Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark
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- Hu, Qiaoxia (author)
- Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark
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- Mahato, Dhani Ram (author)
- Umeå universitet,Umeå University,Kemiska institutionen
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- Longhin, Elena (author)
- Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark
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- Salustros, Nina (author)
- Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark
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- Duelli, Annette (author)
- Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark
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- Lyu, Pin (author)
- Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark
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- Bågenholm, Viktoria (author)
- Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark
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- Eriksson, Jonas (author)
- Umeå universitet,Umeå University,Kemiska institutionen
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- Umashankar Rao, Komal (author)
- 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
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- Henderson, Domhnall Iain (author)
- Department of Laboratory Medicine, Lund University, Klinikgatan 28, Lund, Sweden
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- Meloni, Gabriele (author)
- Department of Chemistry and Biochemistry, The University of Texas at Dallas, 800 W Campbell Rd., TX, Richardson, United States
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- Andersson, Magnus (author)
- Umeå universitet,Umeå University,Kemiska institutionen
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- Croll, Tristan (author)
- Cambridge Institute for Medical Research, Department of Haematology, University of Cambridge, Keith Peters Building, Hills Rd, Cambridge, United Kingdom
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- Godaly, Gabriela (author)
- 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
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- Wang, Kaituo (author)
- Department of Biomedical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen N, Denmark
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- Gourdon, Pontus (author)
- 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
- English 21 s.
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In: eLife. - : eLife Sciences Publications Ltd. - 2050-084X.
- Related links:
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https://doi.org/10.7...
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https://umu.diva-por... (primary) (Raw object)
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https://lup.lub.lu.s...
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https://urn.kb.se/re...
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Abstract
Subject headings
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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.
Subject headings
- 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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- art (subject category)
- ref (subject category)
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eLife
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- By the author/editor
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Grønberg, Christ ...
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Hu, Qiaoxia
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Mahato, Dhani Ra ...
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Longhin, Elena
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Salustros, Nina
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Duelli, Annette
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show more...
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Lyu, Pin
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Bågenholm, Vikto ...
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Eriksson, Jonas
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Umashankar Rao, ...
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Henderson, Domhn ...
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Meloni, Gabriele
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Andersson, Magnu ...
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Croll, Tristan
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Godaly, Gabriela
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Wang, Kaituo
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Gourdon, Pontus
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- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biophysics
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eLife
- By the university
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Lund University
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Umeå University