6UZL
Cryo-EM structure of nucleotide-free MsbA reconstituted into peptidiscs, conformation 2
Summary for 6UZL
| Entry DOI | 10.2210/pdb6uzl/pdb |
| EMDB information | 20950 20959 20962 |
| Descriptor | Lipid A export ATP-binding/permease protein MsbA (1 entity in total) |
| Functional Keywords | membrane protein, abc transporter, membrane mimetic, peptidisc, translocase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 133666.22 |
| Authors | Angiulli, G.,Walz, T.,Dhupar, H.S.,Suzuki, H.,Wason, I.S.,Duong Van Hoa, F. (deposition date: 2019-11-15, release date: 2020-03-04, Last modification date: 2025-05-14) |
| Primary citation | Angiulli, G.,Dhupar, H.S.,Suzuki, H.,Wason, I.S.,Duong Van Hoa, F.,Walz, T. New approach for membrane protein reconstitution into peptidiscs and basis for their adaptability to different proteins. Elife, 9:-, 2020 Cited by PubMed Abstract: 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 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 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. PubMed: 32125274DOI: 10.7554/eLife.53530 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.4 Å) |
Structure validation
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