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9NQJ

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

Summary for 9NQJ
Entry DOI10.2210/pdb9nqj/pdb
EMDB information49659
DescriptorMaltose/maltodextrin import ATP-binding protein MalK, Maltose/maltodextrin transport system permease protein MalF, Maltose/maltodextrin transport system permease protein MalG, ... (6 entities in total)
Functional Keywordsbacterial prototype atp-binding cassette transporter, transport protein
Biological sourceEscherichia coli K-12
More
Total number of polymer chains4
Total formula weight172390.48
Authors
Primary citationRen, Q.,Wang, J.,Idikuda, V.,Zhang, S.,Shin, J.,Ludlam, W.G.,Real Hernandez, L.M.,Zdancewicz, S.,Kreutzberger, A.J.B.,Chang, H.,Kiessling, V.,Tamm, L.K.,Jomaa, A.,Levental, I.,Martemyanov, K.,Chanda, B.,Bao, H.
DeFrND: detergent-free reconstitution into native nanodiscs with designer membrane scaffold peptides.
Nat Commun, 16:7973-7973, 2025
Cited by
PubMed Abstract: 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.
PubMed: 40858559
DOI: 10.1038/s41467-025-63275-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.34 Å)
Structure validation

245663

数据于2025-12-03公开中

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