{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gronberg C"],"funding":["Carlsbergfondet","China Scholarship Council","National Supercomputer Centre","Knut och Alice Wallenbergs Stiftelse","Swedish Research Council","The memorial foundation of manufacturer Vilhelm Pedersen and wife - and the Aarhus Wilson consortium","Lundbeck Foundation","National Institute of General Medical Sciences","Crafoordska Stiftelsen","The Independent Research Fund Denmark","Carl Tryggers Stiftelse för Vetenskaplig Forskning","Brødrene Hartmann","Per-Eric and Ulla Schyberg","Robert A Welch Foundation","Agnes og Poul Friis Fond","Lundbeckfonden","Novo Nordisk Fonden","Augustinus Fonden","Wellcome Trust","NIGMS NIH HHS","National Science Foundation","Swedish Heart-Lung Foundation"],"pagination":["e73124"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8880997"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10"],"pubmed_abstract":["Transition metals, such as zinc, are essential micronutrients in all organisms, but also highly toxic in excessive amounts. Heavy-metal transporting P-type (P<sub>IB</sub>) 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 P<sub>IB-4</sub>-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 P<sub>IB-4</sub>-ATPase, sCoaT from <i>Sulfitobacter</i> 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"],"journal":["eLife"],"pubmed_title":["Structure and ion-release mechanism of P&lt;sub&gt;IB-4&lt;/sub&gt;-type ATPases."],"pmcid":["PMC8880997"],"funding_grant_id":["38267","CF15-0542","R35GM128704","AT-2073-20210327","2013_01_0641","9039-00273A","R35 GM128704","A29519","20200378","R324-2019-1855","CHE-2045984","R133-A12689","2020-03840","R35GM128704)","2020.0194","2015.0131","AT-1935-20170325","16-1992","20180652","2021/5-362","209407/Z/17/Z","CTS 17:22","R313-2019-774","NNF13OC0007471","20170818","218-2016-1548","R263-2017-4406","R139-2012-12689","CHE- 2045984","R218-2016-1548","2016-04474","NNF18SA0034956"],"pubmed_authors":["Gronberg C","Croll T","Godaly G","Mahato DR","Andersson M","Wang K","Duelli A","Bagenholm V","Meloni G","Salustros N","Henderson DI","Longhin E","Eriksson J","Gourdon P","Hu Q","Rao KU","Lyu P"],"additional_accession":[]},"is_claimable":false,"name":"Structure and ion-release mechanism of P&lt;sub&gt;IB-4&lt;/sub&gt;-type ATPases.","description":"Transition metals, such as zinc, are essential micronutrients in all organisms, but also highly toxic in excessive amounts. Heavy-metal transporting P-type (P<sub>IB</sub>) 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 P<sub>IB-4</sub>-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 P<sub>IB-4</sub>-ATPase, sCoaT from <i>Sulfitobacter</i> 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","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Dec","modification":"2026-05-30T15:13:47.924Z","creation":"2025-04-19T22:36:10.173Z"},"accession":"S-EPMC8880997","cross_references":{"pubmed":["34951590"],"doi":["10.7554/eLife.73124"]}}