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dc.contributor.authorGrønberg, Christina
dc.contributor.authorHu, Qiaoxia
dc.contributor.authorMahato, Dhani Ram
dc.contributor.authorLonghin, Elena
dc.contributor.authorSalustros, Nina
dc.contributor.authorDuelli, Annette
dc.contributor.authorLyu, Pin
dc.contributor.authorBågenholm, Viktoria
dc.contributor.authorEriksson, Jonas
dc.contributor.authorRao, Komal Umashankar
dc.contributor.authorHenderson, Domhnall Iain
dc.contributor.authorMeloni, Gabriele
dc.contributor.authorAndersson, Magnus
dc.contributor.authorCroll, Tristan
dc.contributor.authorGodaly, Gabriela
dc.contributor.authorWang, Kaituo
dc.contributor.authorGourdon, Pontus
dc.date.accessioned2022-02-26T03:30:27Z
dc.date.available2022-02-26T03:30:27Z
dc.date.issued2021-12-24
dc.date.submitted2021-08-17
dc.identifier.issn2050-084X
dc.identifier.other73124
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/334474
dc.descriptionFunder: The memorial foundation of manufacturer Vilhelm Pedersen and wife - and the Aarhus Wilson consortium
dc.descriptionFunder: China Scholarship Council; FundRef: http://dx.doi.org/10.13039/501100004543
dc.descriptionFunder: Carl Tryggers Stiftelse för Vetenskaplig Forskning; FundRef: http://dx.doi.org/10.13039/501100002805; Grant(s): CTS 17:22
dc.descriptionFunder: Agnes og Poul Friis Fond; FundRef: http://dx.doi.org/10.13039/100009512
dc.description.abstractTransition metals, such as zinc, are essential micronutrients in all organisms, but also highly toxic in excessive amounts. Heavy-metal transporting P-type (PIB) ATPases are crucial for homeostasis, conferring cellular detoxification and redistribution through transport of these ions across cellular membranes. No structural information is available for the PIB-4-ATPases, the subclass with the broadest cargo scope, and hence even their topology remains elusive. Here, we present structures and complementary functional analyses of an archetypal PIB-4-ATPase, sCoaT from Sulfitobacter 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 and diversity of heavy-metal transporters. We reveal several novel P-type ATPase features, including a dual role in heavy-metal release and as an internal counter ion of an invariant histidine. We also establish that the turnover of PIB-ATPases is potassium independent, contrasting to many other P-type ATPases. Combined with new inhibitory compounds, our results open up for efforts in for example drug discovery, since PIB-4-ATPases function as virulence factors in many pathogens.
dc.languageen
dc.publishereLife Sciences Publications, Ltd
dc.subjectResearch Article
dc.subjectBiochemistry and Chemical Biology
dc.subjectStructural Biology and Molecular Biophysics
dc.subjectP-type ATPase
dc.subjectx-ray crystallography
dc.subjectsulfitobacter sp. NAS14-1
dc.subjecttransition metals
dc.subjectPIB-4-ATPase
dc.subjectOther
dc.titleStructure and ion-release mechanism of PIB-4-type ATPases.
dc.typeArticle
dc.date.updated2022-02-26T03:30:26Z
prism.publicationNameElife
prism.volume10
dc.identifier.doi10.17863/CAM.81891
dcterms.dateAccepted2021-12-17
rioxxterms.versionofrecord10.7554/eLife.73124
rioxxterms.versionVoR
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/
datacite.contributor.supervisoreditor: Maduke, Merritt
datacite.contributor.supervisorsenior_editor: Boudker, Olga
dc.contributor.orcidMahato, Dhani Ram [0000-0002-1121-7761]
dc.contributor.orcidLyu, Pin [0000-0003-4532-0430]
dc.contributor.orcidMeloni, Gabriele [0000-0003-4976-1401]
dc.contributor.orcidAndersson, Magnus [0000-0002-3364-6647]
dc.contributor.orcidCroll, Tristan [0000-0002-3514-8377]
dc.contributor.orcidGodaly, Gabriela [0000-0002-3467-1350]
dc.contributor.orcidGourdon, Pontus [0000-0002-8631-3539]
dc.identifier.eissn2050-084X
pubs.funder-project-idWellcome Trust (209407/Z/17/Z)
cam.issuedOnline2021-12-24


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