1YP8
Solution structure of the cyclotide tricyclon A
Summary for 1YP8
| Entry DOI | 10.2210/pdb1yp8/pdb |
| Descriptor | tricyclon A (1 entity in total) |
| Functional Keywords | beta-sheet, cystine knot, cyclic backbone, cyclotide, cell cycle |
| Biological source | Viola tricolor |
| Total number of polymer chains | 1 |
| Total formula weight | 3506.96 |
| Authors | Mulvenna, J.P.,Sando, L.,Craik, D.J. (deposition date: 2005-01-30, release date: 2005-05-24, Last modification date: 2024-10-09) |
| Primary citation | Mulvenna, J.P.,Sando, L.,Craik, D.J. Processing of a 22 kDa precursor protein to produce the circular protein tricyclon A. Structure, 13:691-701, 2005 Cited by PubMed Abstract: Cyclotides are a family of plant proteins that have the unusual combination of head-to-tail backbone cyclization and a cystine knot motif. They are exceptionally stable and show resistance to most chemical, physical, and enzymatic treatments. The structure of tricyclon A, a previously unreported cyclotide, is described here. In this structure, a loop that is disordered in other cyclotides forms a beta sheet that protrudes from the globular core. This study indicates that the cyclotide fold is amenable to the introduction of a range of structural elements without affecting the cystine knot core of the protein, which is essential for the stability of the cyclotides. Tricyclon A does not possess a hydrophobic patch, typical of other cyclotides, and has minimal hemolytic activity, making it suitable for pharmaceutical applications. The 22 kDa precursor protein of tricyclon A was identified and provides clues to the processing of these fascinating miniproteins. PubMed: 15893660DOI: 10.1016/j.str.2005.02.013 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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