8T1O
AP2 bound to MSP2N2 nanodisc with Tgn38 cargo peptide; composite map
Summary for 8T1O
| Entry DOI | 10.2210/pdb8t1o/pdb |
| EMDB information | 16803 16804 29977 40034 40035 40963 40964 40965 40966 40973 |
| Descriptor | AP-2 complex subunit alpha-2, AP-2 complex subunit beta, AP-2 complex subunit mu, ... (6 entities in total) |
| Functional Keywords | clathrin-mediated endocytosis; peripheral membrane protein, endocytosis |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 5 |
| Total formula weight | 206761.42 |
| 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 citation | S 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: 37364761DOI: 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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