7BCW

Structure of MsbA in Salipro with ADP vanadate

Summary for 7BCW

• Entry DOI: 10.2210/pdb7bcw/pdb
• EMDB information: 12145
• Descriptor: ATP-dependent lipid A-core flippase, VANADATE ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: lipid export msba, membrane protein
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 2
• Total formula weight: 135626.37

Authors

Traore, D.A.K.,Tidow, H. (deposition date: 2020-12-21, release date: 2022-01-12, Last modification date: 2024-07-10)

Primary citation

Kehlenbeck, D.M.,Traore, D.A.K.,Josts, I.,Sander, S.,Moulin, M.,Haertlein, M.,Prevost, S.,Forsyth, V.T.,Tidow, H.
Cryo-EM structure of MsbA in saposin-lipid nanoparticles (Salipro) provides insights into nucleotide coordination.
Febs J., 289:2959-2970, 2022

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 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.

PubMed: 34921499
DOI: 10.1111/febs.16327

Experimental method

ELECTRON MICROSCOPY (3.5 Å)