Journal article

The structural basis of bacterial manganese import

Stephanie L Neville, Jennie Sjoehamn, 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



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 e..

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Awarded by National Health and Medical Research Council (NHMRC)

Awarded by Australian Research Council (ARC)

Awarded by AMED

Awarded by U.S. Department of Energy, Office of Sciences

Awarded by NIH, National Institute of General Medical Sciences

Awarded by LIEF HPC-GPGPU Facility hosted at the University of Melbourne

Awarded by NIH

Funding Acknowledgements

This work was supported by the National Health and Medical Research Council (NHMRC) Project grants 1080784 to C.A.M. and M.J.M.; 1140554 to C.A.M., M.J.M., and M.L.O.; and 1122582 to C.A.M.; an Australian Research Council (ARC) Discovery Project grant DP170102102 to C.A.M.; and funding from the Platform Project for Supporting Drug Discovery and Life Science Research [Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)] from AMED under grant number JP20am0101079 to S.I. (support number 0752). S.L.N. is an NHMRC Early Career Research Fellow (1142695), M.R.D. is a University of Melbourne C. R. Roper Fellow, and C.A.M. and M.J.M. are ARC Future Fellows (FT170100006 and FT180100397, respectively). Part of this study was carried out using the 12-2 beamline at the Stanford Synchrotron Radiation Laboratory (SSRL). We acknowledge travel funding provided by the International Synchrotron Access Program (ISAP) managed by the Australian Synchrotron, part of ANSTO, and funded by the Australian Government. Use of the Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, is supported by the U.S. Department of Energy, Office of Sciences, under contract no. DE-AC02-76SF00515. The SSRL Structural Molecular Biology Program is supported by the DOE Office of Biological and Environmental Research and by the NIH, National Institute of General Medical Sciences (PG0GM133894). The research was undertaken with the assistance of resources and services from the National Computational Infrastructure (NCI), which is supported by the Australian Government, and using the LIEF HPC-GPGPU Facility hosted at the University of Melbourne, established with the assistance of LIEF grant LE170100200. Molecular graphics and analyses were performed with UCSF Chimera, developed by the Resource for Biocomputing, Visualization, and Informatics at the University of California, San Francisco, with support from NIH P41-GM103311. The contents of this publication are solely the responsibility of the authors and do not necessarily represent the official views of NIGMS or NIH.