Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/132681
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Type: | Journal article |
Title: | The structural basis of bacterial manganese import |
Author: | Neville, S.L. Sjöhamn, J. Watts, J.A. MacDermott-Opeskin, H. Fairweather, S.J. Ganio, K. Carey Hulyer, A. McGrath, A.P. Hayes, A.J. Malcolm, T.R. Davies, M.R. Nomura, N. Iwata, S. O'Mara, M.L. Maher, M.J. McDevitt, C.A. |
Citation: | Science Advances, 2021; 7(32):eabg3980-1-eabg3980-11 |
Publisher: | American Association for the Advancement of Science |
Issue Date: | 2021 |
ISSN: | 2375-2548 2375-2548 |
Statement of Responsibility: | Stephanie L. Neville, Jennie Sjöhamn, Jacinta A. Watts, Hugo MacDermott-Opeskin, Stephen J. Fairweather, Katherine Ganio, Alex Carey Hulyer, Aaron P. McGrath, Andrew J. Hayes, Tess R. Malcolm, Mark R. Davies, Norimichi Nomura, So Iwata, Megan L. O’Mara, Megan J. Maher, Christopher A. McDevitt |
Abstract: | 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. |
Rights: | Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). |
DOI: | 10.1126/sciadv.abg3980 |
Grant ID: | http://purl.org/au-research/grants/nhmrc/1080784 http://purl.org/au-research/grants/nhmrc/1140554 http://purl.org/au-research/grants/nhmrc/1122582 http://purl.org/au-research/grants/arc/DP170102102 http://purl.org/au-research/grants/nhmrc/1142695 http://purl.org/au-research/grants/arc/FT170100006 http://purl.org/au-research/grants/arc/FT180100397 http://purl.org/au-research/grants/arc/LE170100200 |
Published version: | http://dx.doi.org/10.1126/sciadv.abg3980 |
Appears in Collections: | Microbiology and Immunology publications |
Files in This Item:
File | Description | Size | Format | |
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hdl_132681.pdf | Published version | 4.07 MB | Adobe PDF | View/Open |
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