{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang Y"],"funding":["NIAID NIH HHS","U.S. Department of Health & Human Services | NIH | Center for Information Technology","NIGMS NIH HHS","U.S. Department of Health & Human Services | National Institutes of Health"],"pagination":["385"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9873690"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(1)"],"pubmed_abstract":["The Zrt-/Irt-like protein (ZIP) family consists of ubiquitously expressed divalent metal transporters critically involved in maintaining systemic and cellular homeostasis of zinc, iron, and manganese. Here, we present a study on a prokaryotic ZIP from Bordetella bronchiseptica (BbZIP) by combining structural biology, evolutionary covariance, computational modeling, and a variety of biochemical assays to tackle the issue of the transport mechanism which has not been established for the ZIP family. The apo state structure in an inward-facing conformation revealed a disassembled transport site, altered inter-helical interactions, and importantly, a rigid body movement of a 4-transmembrane helix (TM) bundle relative to the other TMs. The computationally generated and biochemically validated outward-facing conformation model revealed a slide of the 4-TM bundle, which carries the transport site(s), by approximately 8 Å toward the extracellular side against the static TMs which mediate dimerization. These findings allow us to conclude that BbZIP is an elevator-type transporter."],"journal":["Nature communications"],"pubmed_title":["Structural insights into the elevator-type transport mechanism of a bacterial ZIP metal transporter."],"pmcid":["PMC9873690"],"funding_grant_id":["R35 GM140931","GM140931","GM129004","GM126189","AI164266","R01 GM126189","R01 GM129004","R01 AI164266"],"pubmed_authors":["Jiang Y","Wei GW","Sui D","Hu J","Zhang Y","Gao K","Yu P","Su M"],"additional_accession":[]},"is_claimable":false,"name":"Structural insights into the elevator-type transport mechanism of a bacterial ZIP metal transporter.","description":"The Zrt-/Irt-like protein (ZIP) family consists of ubiquitously expressed divalent metal transporters critically involved in maintaining systemic and cellular homeostasis of zinc, iron, and manganese. Here, we present a study on a prokaryotic ZIP from Bordetella bronchiseptica (BbZIP) by combining structural biology, evolutionary covariance, computational modeling, and a variety of biochemical assays to tackle the issue of the transport mechanism which has not been established for the ZIP family. The apo state structure in an inward-facing conformation revealed a disassembled transport site, altered inter-helical interactions, and importantly, a rigid body movement of a 4-transmembrane helix (TM) bundle relative to the other TMs. The computationally generated and biochemically validated outward-facing conformation model revealed a slide of the 4-TM bundle, which carries the transport site(s), by approximately 8 Å toward the extracellular side against the static TMs which mediate dimerization. These findings allow us to conclude that BbZIP is an elevator-type transporter.","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jan","modification":"2026-05-10T06:58:12.579Z","creation":"2025-04-05T20:20:35.6Z"},"accession":"S-EPMC9873690","cross_references":{"pubmed":["36693843"],"doi":["10.1038/s41467-023-36048-4"]}}