Structural highlights
FunctionMSBA_ECOLI Involved in lipid A export and possibly also in glycerophospholipid export and for biogenesis of the outer membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation. Publication Abstract from PubMedHigh-resolution structure determination of membrane proteins typically requires reconstitution into artificial membrane mimics. The choice of the specific membrane substitute can strongly affect the protein's specific activity, stability, and conformational spectrum, potentially leading to errors or misinterpretation during analysis. The bacterial ATP-binding cassette transporter MsbA is a prominent example of such environment-specific bias. Here, we present a systematic analysis of the conformational spectrum of MsbA, stabilized in a dozen environments, using cryoelectron microscopy (cryo-EM), and show pronounced feedback between the membrane mimetics and the transporter. Detergents generally favor wide inward-facing conformations while nanodiscs induce narrower conformations. Notably, only in three tested environments, MsbA samples the full movement of the nucleotide-binding domains, including narrow and wide conformations. We expect this study to serve as a blueprint for other membrane proteins, even where a structural reaction to the hydrophobic environment is not directly visible but still critical for the proteins' function. The ABC transporter MsbA in a dozen environments.,Hoffmann L, Baier A, Jorde L, Kamel M, Schafer JH, Schnelle K, Scholz A, Shvarev D, Wong JEMM, Parey K, Januliene D, Moeller A Structure. 2025 Feb 28:S0969-2126(25)00055-3. doi: 10.1016/j.str.2025.02.002. PMID:40056915[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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