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dc.contributor.authorBozzi, Aaron Thomas
dc.contributor.authorBane, Lukas Blackford
dc.contributor.authorWeihofen, Wilhelm A.
dc.contributor.authorSingharoy, Abhishek
dc.contributor.authorGuillen, Eduardo R.
dc.contributor.authorPloegh, Hidde L.
dc.contributor.authorSchulten, Klaus
dc.contributor.authorGaudet, Rachelle
dc.date.accessioned2017-05-16T15:40:43Z
dash.embargo.terms2017-12-07
dc.date.issued2016
dc.identifierQuick submit: 2016-10-18T16:42:06-0400
dc.identifier.citationBozzi, Aaron T., Lukas B. Bane, Wilhelm A. Weihofen, Abhishek Singharoy, Eduardo R. Guillen, Hidde L. Ploegh, Klaus Schulten, and Rachelle Gaudet. 2016. “Crystal Structure and Conformational Change Mechanism of a Bacterial Nramp-Family Divalent Metal Transporter.” Structure 24 (12) (December): 2102–2114. doi:10.1016/j.str.2016.09.017.en_US
dc.identifier.issn0969-2126en_US
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:32689445
dc.description.abstractThe widely-conserved natural resistance associated macrophage protein (Nramp) family of divalent metal transporters enables manganese import in bacteria and dietary iron uptake in mammals. We determined the crystal structure of the Deinococcus radiodurans Nramp homolog (DraNramp) in an inward-facing apo state, including the complete transmembrane (TM) segment 1a—absent from a previous Nramp structure. Mapping our cysteine accessibility scanning results onto this structure, we identified the metal permeation pathway in the alternate outward-open conformation. We investigated the functional impact of two natural anemia-causing glycine-toarginine mutations, which impaired transition metal transport in both human Nramp2 and DraNramp. The TM4 G153R mutation perturbs the closing of the outward metal permeation pathway and alters the selectivity of the conserved metal-binding site. In contrast, the TM1a G45R mutation prevents conformational change by sterically blocking the essential movement of that helix, thus locking the transporter in an inward-facing state.en_US
dc.description.sponsorshipMolecular and Cellular Biologyen_US
dc.language.isoen_USen_US
dc.publisherElsevier BVen_US
dc.relation.isversionofdoi:10.1016/j.str.2016.09.017en_US
dash.licenseLAA
dc.titleCrystal Structure and Conformational Change Mechanism of a Bacterial Nramp-Family Divalent Metal Transporteren_US
dc.typeJournal Articleen_US
dc.date.updated2016-10-18T20:42:12Z
dc.description.versionAccepted Manuscripten_US
dc.relation.journalStructureen_US
dash.depositing.authorGaudet, Rachelle
dash.waiver2016-10-18
dc.date.available2017-12-07T08:30:58Z
dc.identifier.doi10.1016/j.str.2016.09.017*
dash.contributor.affiliatedBozzi, Aaron
dash.contributor.affiliatedBane, Lukas Blackford
dash.contributor.affiliatedGaudet, Rachelle


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