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Title | Cryo-EM structure of MsbA in saposin-lipid nanoparticles (Salipro) provides insights into nucleotide coordination. |
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Journal, issue, pages | FEBS J, Vol. 289, Issue 10, Page 2959-2970, Year 2022 |
Publish date | Dec 17, 2021 |
Authors | Dominique-Maurice Kehlenbeck / Daouda A K Traore / Inokentijs Josts / Simon Sander / Martine Moulin / Michael Haertlein / Sylvain Prevost / V Trevor Forsyth / Henning Tidow / |
PubMed Abstract | The ATP-binding cassette transporter MsbA is a lipid flippase, translocating lipid A, glycolipids, and lipopolysaccharides from the inner to the outer leaflet of the inner membrane of Gram-negative ...The ATP-binding cassette transporter MsbA is a lipid flippase, translocating lipid A, glycolipids, and lipopolysaccharides from the inner to the outer leaflet of the inner membrane of Gram-negative bacteria. It has been used as a model system for time-resolved structural studies as several MsbA structures in different states and reconstitution systems (detergent/nanodiscs/peptidiscs) are available. However, due to the limited resolution of the available structures, detailed structural information on the bound nucleotides has remained elusive. Here, we have reconstituted MsbA in saposin A-lipoprotein nanoparticles (Salipro) and determined the structure of ADP-vanadate-bound MsbA by single-particle cryo-electron microscopy to 3.5 Å resolution. This procedure has resulted in significantly improved resolution and enabled us to model all side chains and visualise detailed ADP-vanadate interactions in the nucleotide-binding domains. The approach may be applicable to other dynamic membrane proteins. |
External links | FEBS J / PubMed:34921499 |
Methods | EM (single particle) |
Resolution | 3.5 Å |
Structure data | EMDB-12145, PDB-7bcw: |
Chemicals | ChemComp-VO4: ChemComp-ADP: ChemComp-MG: ChemComp-POV: |
Source |
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Keywords | MEMBRANE PROTEIN / Lipid export MsbA |