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-Structure paper
タイトル | Cryo-EM structure of MsbA in saposin-lipid nanoparticles (Salipro) provides insights into nucleotide coordination. |
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ジャーナル・号・ページ | FEBS J, Vol. 289, Issue 10, Page 2959-2970, Year 2022 |
掲載日 | 2021年12月27日 |
著者 | Dominique-Maurice Kehlenbeck / Daouda A K Traore / Inokentijs Josts / Simon Sander / Martine Moulin / Michael Haertlein / Sylvain Prevost / V Trevor Forsyth / Henning Tidow / |
PubMed 要旨 | 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. |
リンク | FEBS J / PubMed:34921499 |
手法 | EM (単粒子) |
解像度 | 3.5 Å |
構造データ | EMDB-12145, PDB-7bcw: |
化合物 | ChemComp-VO4: ChemComp-ADP: ChemComp-MG: ChemComp-POV: |
由来 |
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キーワード | MEMBRANE PROTEIN / Lipid export MsbA |