Crystal structure of an archaeal CorB magnesium transporter

Yu Seby Chen, Guennadi Kozlov, Brandon E. Moeller, Ahmed Rohaim, Rayan Fakih, Benoît Roux, John E. Burke and Kalle Gehring ()
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Yu Seby Chen: McGill University
Guennadi Kozlov: McGill University
Brandon E. Moeller: University of Victoria
Ahmed Rohaim: University of Chicago, Gordon Center for Integrative Science
Rayan Fakih: McGill University
Benoît Roux: University of Chicago, Gordon Center for Integrative Science
John E. Burke: University of Victoria
Kalle Gehring: McGill University

Nature Communications, 2021, vol. 12, issue 1, 1-14

Abstract: Abstract CNNM/CorB proteins are a broadly conserved family of integral membrane proteins with close to 90,000 protein sequences known. They are associated with Mg2+ transport but it is not known if they mediate transport themselves or regulate other transporters. Here, we determine the crystal structure of an archaeal CorB protein in two conformations (apo and Mg2+-ATP bound). The transmembrane DUF21 domain exists in an inward-facing conformation with a Mg2+ ion coordinated by a conserved π-helix. In the absence of Mg2+-ATP, the CBS-pair domain adopts an elongated dimeric configuration with previously unobserved domain-domain contacts. Hydrogen-deuterium exchange mass spectrometry, analytical ultracentrifugation, and molecular dynamics experiments support a role of the structural rearrangements in mediating Mg2+-ATP sensing. Lastly, we use an in vitro, liposome-based assay to demonstrate direct Mg2+ transport by CorB proteins. These structural and functional insights provide a framework for understanding function of CNNMs in Mg2+ transport and associated diseases.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24282-7

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DOI: 10.1038/s41467-021-24282-7

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