Nature Communications (Feb 2023)
Structure and mechanism of a tripartite ATP-independent periplasmic TRAP transporter
- James S. Davies,
- Michael J. Currie,
- Rachel A. North,
- Mariafrancesca Scalise,
- Joshua D. Wright,
- Jack M. Copping,
- Daniela M. Remus,
- Ashutosh Gulati,
- Dustin R. Morado,
- Sam A. Jamieson,
- Michael C. Newton-Vesty,
- Gayan S. Abeysekera,
- Subramanian Ramaswamy,
- Rosmarie Friemann,
- Soichi Wakatsuki,
- Jane R. Allison,
- Cesare Indiveri,
- David Drew,
- Peter D. Mace,
- Renwick C. J. Dobson
Affiliations
- James S. Davies
- Biomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology and School of Biological Sciences, University of Canterbury
- Michael J. Currie
- Biomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology and School of Biological Sciences, University of Canterbury
- Rachel A. North
- Biomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology and School of Biological Sciences, University of Canterbury
- Mariafrancesca Scalise
- Department DiBEST (Biologia, Ecologia, Scienze della Terra) Unit of Biochemistry and Molecular Biotechnology, University of Calabria
- Joshua D. Wright
- Biomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology and School of Biological Sciences, University of Canterbury
- Jack M. Copping
- Biomolecular Interaction Centre, Digital Life Institute, Maurice Wilkins Centre for Molecular Biodiscovery, and School of Biological Sciences, University of Auckland
- Daniela M. Remus
- Biomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology and School of Biological Sciences, University of Canterbury
- Ashutosh Gulati
- Department of Biochemistry and Biophysics, Stockholm University
- Dustin R. Morado
- Science for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University
- Sam A. Jamieson
- Biochemistry Department, School of Biomedical Sciences, University of Otago
- Michael C. Newton-Vesty
- Biomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology and School of Biological Sciences, University of Canterbury
- Gayan S. Abeysekera
- Biomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology and School of Biological Sciences, University of Canterbury
- Subramanian Ramaswamy
- Biological Sciences and Biomedical Engineering, Bindley Bioscience Center, Purdue University
- Rosmarie Friemann
- Centre for Antibiotic Resistance Research (CARe) at University of Gothenburg
- Soichi Wakatsuki
- Biological Sciences Division, SLAC National Accelerator Laboratory
- Jane R. Allison
- Biomolecular Interaction Centre, Digital Life Institute, Maurice Wilkins Centre for Molecular Biodiscovery, and School of Biological Sciences, University of Auckland
- Cesare Indiveri
- Department DiBEST (Biologia, Ecologia, Scienze della Terra) Unit of Biochemistry and Molecular Biotechnology, University of Calabria
- David Drew
- Department of Biochemistry and Biophysics, Stockholm University
- Peter D. Mace
- Biochemistry Department, School of Biomedical Sciences, University of Otago
- Renwick C. J. Dobson
- Biomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology and School of Biological Sciences, University of Canterbury
- DOI
- https://doi.org/10.1038/s41467-023-36590-1
- Journal volume & issue
-
Vol. 14,
no. 1
pp. 1 – 12
Abstract
Bacteria and archaea use tripartite ATP-independent periplasmic (TRAP) transporters to import essential nutrients. Davies et al. report a high resolution structure of a TRAP and show that it uses an ‘elevator-with-an operator’ mechanism.