The structural basis of bacterial manganese import
| Autor: | Katherine Ganio, Andrew J. Hayes, Norimichi Nomura, Christopher A. McDevitt, Alex Carey Hulyer, Stephen J. Fairweather, Megan J. Maher, Tess R. Malcolm, Jacinta A. Watts, Aaron P. McGrath, Megan L. O'Mara, So Iwata, Jennie Sjöhamn, Stephanie L. Neville, Mark R. Davies, Hugo MacDermott-Opeskin |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences Multidisciplinary 010304 chemical physics Permease Mutagenesis Biophysics chemistry.chemical_element SciAdv r-articles Transporter ATP-binding cassette transporter Manganese 01 natural sciences Transmembrane protein Divalent 03 medical and health sciences chemistry Structural Biology 0103 physical sciences Extracellular Research Articles 030304 developmental biology Research Article |
| Zdroj: | Science Advances |
| ISSN: | 2375-2548 |
| Popis: | Bacterial manganese import is achieved by unique architectural features that are conserved across the kingdoms of life. 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. Here, we present 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. Mutagenesis of the extracellular gate perturbs manganese uptake, while coordination site mutagenesis abolishes import. 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. |
| Databáze: | OpenAIRE |
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