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Structure and Cooperativity of the Cytosolic Domain of the CorA Mg2+ Channel from Escherichia coli
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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Number of Authors: 5
2017 (English)In: Structure, ISSN 0969-2126, E-ISSN 1878-4186, Vol. 25, no 8, 1175-1186.e4 p.Article in journal (Refereed) Published
Abstract [en]

Structures of the Mg2+ bound (closed) and apo (open) states of CorA suggests that channel gating is accomplished by rigid-body motions between symmetric and asymmetric assemblies of the cytosolic portions of the five subunits in response to ligand (Mg2+) binding/unbinding at interfacial sites. Here, we structurally and biochemically characterize the isolated cytosolic domain from Escherichia coli CorA. The data reveal an Mg2+-ligand binding site located in a novel position between each of the five subunits and two Mg2+ ions trapped inside the pore. Soaking experiments show that cobalt hexammine outcompetes Mg2+ at the pore site closest to the membrane. This represents the first structural information of how an analog of hexa-hydrated Mg2+ (and competitive inhibitor of CorA) associates to the CorA pore. Biochemical data on the isolated cytoplasmic domain and full-length protein suggests that gating of the CorA channel is governed cooperatively.

Place, publisher, year, edition, pages
2017. Vol. 25, no 8, 1175-1186.e4 p.
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Biological Sciences
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URN: urn:nbn:se:su:diva-147148DOI: 10.1016/j.str.2017.05.024ISI: 000406744600002PubMedID: 28669631OAI: oai:DiVA.org:su-147148DiVA: diva2:1144061
Available from: 2017-09-25 Created: 2017-09-25 Last updated: 2017-09-25Bibliographically approved

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Lerche, MichaelSandhu, HenaHögbom, MartinRapp, Mikaela
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