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The structural basis of bacterial manganese import

Journal Article · · Science Advances
 [1];  [2];  [1];  [3];  [4];  [1];  [1];  [2];  [1];  [5];  [1];  [6];  [7];  [3];  [8];  [1]
  1. Department of Microbiology and Immunology, The Peter Doherty Institute for Infection and Immunity, The University of Melbourne, Melbourne, Victoria, Australia.
  2. Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Victoria, Australia.
  3. Research School of Chemistry, Australian National University, Canberra, ACT, Australia.
  4. Research School of Chemistry, Australian National University, Canberra, ACT, Australia., Research School of Biology, Australian National University, Canberra, ACT, Australia.
  5. School of Chemistry and The Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Melbourne, Victoria, Australia.
  6. Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
  7. Department of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan., Research Acceleration Program, Membrane Protein Crystallography Project, Japan Science and Technology Agency, Kyoto, Japan., RIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo, Japan.
  8. Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Victoria, Australia., School of Chemistry and The Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Melbourne, Victoria, Australia.

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.

Research Organization:
SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
Sponsoring Organization:
USDOE; USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities Division
Grant/Contract Number:
AC02-76SF00515
OSTI ID:
1812253
Alternate ID(s):
OSTI ID: 1812256
OSTI ID: 1816274
Journal Information:
Science Advances, Journal Name: Science Advances Journal Issue: 32 Vol. 7; ISSN 2375-2548
Publisher:
American Association for the Advancement of Science (AAAS)Copyright Statement
Country of Publication:
United States
Language:
English

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