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-Structure paper
タイトル | The ABC transporter MsbA adopts the wide inward-open conformation in cells. |
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ジャーナル・号・ページ | Sci Adv, Vol. 8, Issue 41, Page eabn6845, Year 2022 |
掲載日 | 2022年10月14日 |
著者 | Laura Galazzo / Gianmarco Meier / Dovile Januliene / Kristian Parey / Dario De Vecchis / Bianca Striednig / Hubert Hilbi / Lars V Schäfer / Ilya Kuprov / Arne Moeller / Enrica Bordignon / Markus A Seeger / |
PubMed 要旨 | Membrane proteins are currently investigated after detergent extraction from native cellular membranes and reconstitution into artificial liposomes or nanodiscs, thereby removing them from their ...Membrane proteins are currently investigated after detergent extraction from native cellular membranes and reconstitution into artificial liposomes or nanodiscs, thereby removing them from their physiological environment. However, to truly understand the biophysical properties of membrane proteins in a physiological environment, they must be investigated within living cells. Here, we used a spin-labeled nanobody to interrogate the conformational cycle of the ABC transporter MsbA by double electron-electron resonance. Unexpectedly, the wide inward-open conformation of MsbA, commonly considered a nonphysiological state, was found to be prominently populated in cells. Molecular dynamics simulations revealed that extensive lateral portal opening is essential to provide access of its large natural substrate core lipid A to the binding cavity. Our work paves the way to investigate the conformational landscape of membrane proteins in cells. |
リンク | Sci Adv / PubMed:36223470 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 2.1 - 4.1 Å |
構造データ | EMDB-13404, PDB-7ph2: EMDB-13405, PDB-7ph3: EMDB-13406, PDB-7ph4: EMDB-13409, PDB-7ph7: PDB-7ndf: |
化合物 | ChemComp-HOH: ChemComp-EIW: ChemComp-88T: ChemComp-GD: ChemComp-ANP: ChemComp-MG: ChemComp-LMT: ChemComp-3PE: |
由来 |
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キーワード | PROTEIN BINDING / nucleotide binding domain / ABC transporter / nanobody / MEMBRANE PROTEIN / Gd-DOTA / AMP-PNP / lipid A |