Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	New approach for membrane protein reconstitution into peptidiscs and basis for their adaptability to different proteins.
Journal, issue, pages	Elife, Vol. 9, Year 2020
Publish date	Mar 3, 2020
Authors	Gabriella Angiulli / Harveer Singh Dhupar / Hiroshi Suzuki / Irvinder Singh Wason / Franck Duong Van Hoa / Thomas Walz /
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 ...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.
External links	Elife / PubMed:32125274 / PubMed Central
Methods	EM (single particle)
Resolution	3.3 - 4.4 Å
Structure data	20950 6uz2 EMDB-20950, PDB-6uz2: Cryo-EM structure of nucleotide-free MsbA reconstituted into peptidiscs, conformation 1 Method: EM (single particle) / Resolution: 4.2 Å 20959 6uzh EMDB-20959: Cryo-EM structure of the mechanosensitive channel MscS reconstituted into peptidiscs PDB-6uzh: Cryo-EM structure of mechanosensitive channel MscS reconstituted into peptidiscs Method: EM (single particle) / Resolution: 3.3 Å 20962 6uzl EMDB-20962, PDB-6uzl: Cryo-EM structure of nucleotide-free MsbA reconstituted into peptidiscs, conformation 2 Method: EM (single particle) / Resolution: 4.4 Å
Source	escherichia coli (E. coli)
Keywords	TRANSLOCASE / membrane protein / ABC transporter / membrane mimetic / peptidisc / TRANSPORT PROTEIN / mechanosensitive channels / MscS