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8T1O

AP2 bound to MSP2N2 nanodisc with Tgn38 cargo peptide; composite map

Summary for 8T1O
Entry DOI10.2210/pdb8t1o/pdb
EMDB information16803 16804 29977 40034 40035 40963 40964 40965 40966 40973
DescriptorAP-2 complex subunit alpha-2, AP-2 complex subunit beta, AP-2 complex subunit mu, ... (6 entities in total)
Functional Keywordsclathrin-mediated endocytosis; peripheral membrane protein, endocytosis
Biological sourceMus musculus (house mouse)
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Total number of polymer chains5
Total formula weight206761.42
Authors
Baker, R.W.,Cannon, K.S.,Reta, S. (deposition date: 2023-06-02, release date: 2023-07-12, Last modification date: 2025-05-21)
Primary citationS Cannon, K.,Sarsam, R.D.,Tedamrongwanish, T.,Zhang, K.,Baker, R.W.
Lipid nanodiscs as a template for high-resolution cryo-EM structures of peripheral membrane proteins.
J.Struct.Biol., 215:107989-107989, 2023
Cited by
PubMed 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.
PubMed: 37364761
DOI: 10.1016/j.jsb.2023.107989
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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