9nqj

Cryo-EM structure of a bacterial prototype ATP-binding cassette transporter MalFGK2.

spinqualitylabelsall models 9nqj, resolution 3.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9nqj is a 4 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.34Å Ligands: ADP, MG, VO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MALK_ECOLI Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system. Publication Abstract from PubMed Membrane scaffold protein-based nanodiscs have facilitated unprecedented structural and biophysical analysis of membrane proteins in a near-native lipid environment. However, successful reconstitution of membrane proteins in nanodiscs requires prior solubilization and purification in detergents, which may impact their physiological structure and function. Furthermore, the detergent-mediated reconstitution of nanodiscs is unlikely to recapitulate the precise composition or asymmetry of native membranes. To circumvent this fundamental limitation of traditional nanodisc technology, we herein describe the development of membrane-solubilizing peptides to directly extract membrane proteins from native cell membranes into nanoscale discoids. By systematically protein engineering and screening, we create a class of chemically modified Apolipoprotein-A1 mimetic peptides to enable the formation of detergent-free nanodiscs with high efficiency. Nanodiscs generated with these engineered membrane scaffold peptides are suitable for obtaining high-resolution structures using single-particle cryo-EM with native lipids. To further highlight the versatility of our approach, we directly extract a sampling of membrane signaling proteins with their surrounding native membranes for biochemical and biophysical interrogations. DeFrND: detergent-free reconstitution into native nanodiscs with designer membrane scaffold peptides.,Ren Q, Wang J, Idikuda V, Zhang S, Shin J, Ludlam WG, Real Hernandez LM, Zdancewicz S, Kreutzberger AJB, Chang H, Kiessling V, Tamm LK, Jomaa A, Levental I, Martemyanov K, Chanda B, Bao H Nat Commun. 2025 Aug 26;16(1):7973. doi: 10.1038/s41467-025-63275-8. PMID:40858559 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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