8EAW
An asymmetric disk assembly formed by tandem dimers of the tobacco mosaic viral capsid protein (TMV)
Summary for 8EAW
| Entry DOI | 10.2210/pdb8eaw/pdb |
| Descriptor | Capsid protein (1 entity in total) |
| Functional Keywords | viral capsid proteins, tobacco mosaic virus, protein assembly, viral protein |
| Biological source | Tobacco mosaic virus (vulgare) More |
| Total number of polymer chains | 17 |
| Total formula weight | 603438.71 |
| Authors | Dai, J.,Pereira, J.H.,Adams, P.D.,Francis, M.B. (deposition date: 2022-08-29, release date: 2023-03-01, Last modification date: 2024-05-01) |
| Primary citation | Dai, J.,Wilhelm, K.B.,Bischoff, A.J.,Pereira, J.H.,Dedeo, M.T.,Garcia-Almedina, D.M.,Adams, P.D.,Groves, J.T.,Francis, M.B. A Membrane-Associated Light-Harvesting Model is Enabled by Functionalized Assemblies of Gene-Doubled TMV Proteins. Small, 19:e2207805-e2207805, 2023 Cited by PubMed Abstract: Photosynthetic light harvesting requires efficient energy transfer within dynamic networks of light-harvesting complexes embedded within phospholipid membranes. Artificial light-harvesting models are valuable tools for understanding the structural features underpinning energy absorption and transfer within chromophore arrays. Here, a method for attaching a protein-based light-harvesting model to a planar, fluid supported lipid bilayer (SLB) is developed. The protein model consists of the tobacco mosaic viral capsid proteins that are gene-doubled to create a tandem dimer (dTMV). Assemblies of dTMV break the facial symmetry of the double disk to allow for differentiation between the disk faces. A single reactive lysine residue is incorporated into the dTMV assemblies for the site-selective attachment of chromophores for light absorption. On the opposing dTMV face, a cysteine residue is incorporated for the bioconjugation of a peptide containing a polyhistidine tag for association with SLBs. The dual-modified dTMV complexes show significant association with SLBs and exhibit mobility on the bilayer. The techniques used herein offer a new method for protein-surface attachment and provide a platform for evaluating excited state energy transfer events in a dynamic, fully synthetic artificial light-harvesting system. PubMed: 36811150DOI: 10.1002/smll.202207805 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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