The structural basis of bacterial manganese import

Stephanie L Neville, Jennie Sjöhamn, Jacinta A. Watts, Hugo Macdermott-Opeskin, Stephen Fairweather, Katherine Ganio, Alex Carey Hulyer, Andrew J. Hayes, Aaron P. McGrath, Tess R. Malcolm, Mark R. Davies, Norimichi Nomura, Megan O'Mara

    Research output: Contribution to journalArticle


    Metal ions are essential for all forms of life. In prokaryotes, ATP-binding cassette (ABC) permeases serve as the primary import pathway for many micronutrients including the first-row transition metal manganese. However, the structural features of ionic metal transporting ABC permeases have remained undefined. This presentation will describe the crystal structure of the manganese transporter PsaBC from Streptococcus pneumoniae in an open-inward conformation. The Type II transporter has a tightly closed transmembrane channel due to extracellular gating residues that prevent water permeation or ion reflux. Below these residues, the channel contains a hitherto unreported metal coordination site, which is essential for manganese translocation. These structural features are highly conserved in metal-specific ABC transporters and are represented throughout the kingdoms of life. Collectively, our results define the structure of PsaBC and reveal the features required for divalent cation transport
    Original languageEnglish
    JournalScience Advances
    Publication statusPublished - 2022


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