8XWG
OspA variants for thioflavin-T binding
Summary for 8XWG
| Entry DOI | 10.2210/pdb8xwg/pdb |
| Descriptor | Outer Surface Protein A (2 entities in total) |
| Functional Keywords | beta-sheet, thioflavin-t, amyloid, unknown function |
| Biological source | Borreliella burgdorferi (Lyme disease spirochete) |
| Total number of polymer chains | 1 |
| Total formula weight | 34488.41 |
| Authors | |
| Primary citation | Miura, Y.,Namioka, S.,Iwai, A.,Yoshida, N.,Konno, H.,Sohma, Y.,Kanai, M.,Makabe, K. Redesign of a thioflavin-T-binding protein with a flat beta-sheet to evaluate a thioflavin-T-derived photocatalyst with enhanced affinity. Int.J.Biol.Macromol., 269:131992-131992, 2024 Cited by PubMed Abstract: Amyloids, proteinous aggregates with β-sheet-rich fibrils, are involved in several neurodegenerative diseases such as Alzheimer's disease; thus, their detection is critically important. The most common fluorescent dye for amyloid detection is thioflavin-T (ThT), which shows on/off fluorescence upon amyloid binding. We previously reported that an engineered globular protein with a flat β-sheet, peptide self-assembly mimic (PSAM), can be used as an amyloid binding model. In this study, we further explored the residue-specific properties of ThT-binding to the flat β-sheet by introducing systematic mutations. We found that site-specific mutations at the ThT-binding channel enhanced affinity. We also evaluated the binding of a ThT-based photocatalyst, which showed the photooxygenation activity on the amyloid fibril upon light radiation. Upon binding of the photocatalyst to the PSAM variant, singlet oxygen-generating activity was observed. The results of this study expand our understanding of the detailed binding mechanism of amyloid-specific molecules. PubMed: 38697433DOI: 10.1016/j.ijbiomac.2024.131992 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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