EMD-29977

Single-particle
4.2 Å
EMD-29977 Deposition: 07/03/2023
Map released: 12/07/2023
Last modified: 19/07/2023
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-29977

AP2 bound to an MSP1 nanodisc

EMD-29977

Single-particle
4.2 Å
EMD-29977 Deposition: 07/03/2023
Map released: 12/07/2023
Last modified: 19/07/2023
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Mus musculus, Homo sapiens
Sample: AP2 bound to MSP2N2 nanodisc
Raw data: EMPIAR-11455

Deposition Authors: Sarsam RD , Cannon KS , Baker RW
Lipid nanodiscs as a template for high-resolution cryo-EM structures of peripheral membrane proteins.
S Cannon K, Sarsam RD , Tedamrongwanish T, Zhang K, Baker RW
(2023) J Struct Biol , 215 , 107989 - 107989
PUBMED: 37364761
DOI: doi:10.1016/j.jsb.2023.107989
ISSN: 1095-8657
ASTM: JSBIEM
Abstract:
Peripheral membrane proteins are ubiquitous throughout cell biology and are required for a variety of cellular processes such as signal transduction, membrane trafficking, and autophagy. Transient binding to the membrane has a profound impact on protein function, serving to induce conformational changes and alter biochemical and biophysical parameters by increasing the local concentration of factors and restricting diffusion to two dimensions. Despite the centrality of the membrane in serving as a template for cell biology, there are few reported high-resolution structures of peripheral membrane proteins bound to the membrane. We analyzed the utility of lipid nanodiscs to serve as a template for cryo-EM analysis of peripheral membrane proteins. We tested a variety of nanodiscs and we report a 3.3 Å structure of the AP2 clathrin adaptor complex bound to a 17-nm nanodisc, with sufficient resolution to visualize a bound lipid head group. Our data demonstrate that lipid nanodiscs are amenable to high-resolution structure determination of peripheral membrane proteins and provide a framework for extending this analysis to other systems.