6uz2: Difference between revisions
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/MSBA_ECOLI MSBA_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. | [https://www.uniprot.org/uniprot/MSBA_ECOLI MSBA_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. | ||
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== Publication Abstract from PubMed == | |||
Previously we introduced peptidiscs as an alternative to detergents to stabilize membrane proteins in solution (Carlson et al., 2018). Here, we present 'on-gradient' reconstitution, a new gentle approach for the reconstitution of labile membrane-protein complexes, and used it to reconstitute Rhodobacter sphaeroides reaction center complexes, demonstrating that peptidiscs can adapt to transmembrane domains of very different sizes and shapes. Using the conventional 'on-bead' approach, we reconstituted Escherichia coli proteins MsbA and MscS and find that peptidiscs stabilize them in their native conformation and allow for high-resolution structure determination by cryo-electron microscopy. The structures reveal that peptidisc peptides can arrange around transmembrane proteins differently, thus revealing the structural basis for why peptidiscs can stabilize such a large variety of membrane proteins. Together, our results establish the gentle and easy-to-use peptidiscs as a potentially universal alternative to detergents as a means to stabilize membrane proteins in solution for structural and functional studies. | |||
New approach for membrane protein reconstitution into peptidiscs and basis for their adaptability to different proteins.,Angiulli G, Dhupar HS, Suzuki H, Wason IS, Duong Van Hoa F, Walz T Elife. 2020 Mar 3;9. pii: 53530. doi: 10.7554/eLife.53530. PMID:32125274<ref>PMID:32125274</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
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Latest revision as of 05:57, 14 May 2025
Cryo-EM structure of nucleotide-free MsbA reconstituted into peptidiscs, conformation 1
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