Nature Communications (Aug 2022)
Structural and mechanistic analysis of a tripartite ATP-independent periplasmic TRAP transporter
- Martin F. Peter,
- Jan A. Ruland,
- Peer Depping,
- Niels Schneberger,
- Emmanuele Severi,
- Jonas Moecking,
- Karl Gatterdam,
- Sarah Tindall,
- Alexandre Durand,
- Veronika Heinz,
- Jan Peter Siebrasse,
- Paul-Albert Koenig,
- Matthias Geyer,
- Christine Ziegler,
- Ulrich Kubitscheck,
- Gavin H. Thomas,
- Gregor Hagelueken
Affiliations
- Martin F. Peter
- Institute of Structural Biology, University of Bonn
- Jan A. Ruland
- Institute for Physical und Theoretical Chemistry, University of Bonn
- Peer Depping
- Institute of Structural Biology, University of Bonn
- Niels Schneberger
- Institute of Structural Biology, University of Bonn
- Emmanuele Severi
- Department of Biology (Area 10), University of York
- Jonas Moecking
- Institute of Structural Biology, University of Bonn
- Karl Gatterdam
- Institute of Structural Biology, University of Bonn
- Sarah Tindall
- Department of Biology (Area 10), University of York
- Alexandre Durand
- Institut de Génétique et de Biologie Molecule et Cellulaire
- Veronika Heinz
- Institute of Biophysics and Biophysical Chemistry, University of Regensburg
- Jan Peter Siebrasse
- Institute for Physical und Theoretical Chemistry, University of Bonn
- Paul-Albert Koenig
- Core Facility Nanobodies, University of Bonn
- Matthias Geyer
- Institute of Structural Biology, University of Bonn
- Christine Ziegler
- Institute of Biophysics and Biophysical Chemistry, University of Regensburg
- Ulrich Kubitscheck
- Institute for Physical und Theoretical Chemistry, University of Bonn
- Gavin H. Thomas
- Department of Biology (Area 10), University of York
- Gregor Hagelueken
- Institute of Structural Biology, University of Bonn
- DOI
- https://doi.org/10.1038/s41467-022-31907-y
- Journal volume & issue
-
Vol. 13,
no. 1
pp. 1 – 15
Abstract
Tripartite ATP-independent periplasmic (TRAP) transporters are widespread in bacteria and archaea. Here, the authors used cryo-EM and a range of biophysical techniques to study the structure of function of the sialic acid TRAP transporter HiSiaQM.
