5FZQ
Designed TPR Protein M4N
Summary for 5FZQ
| Entry DOI | 10.2210/pdb5fzq/pdb |
| Related | 5FZR 5FZS |
| Descriptor | DESIGNED TPR PROTEIN, SULFATE ION (3 entities in total) |
| Functional Keywords | unknown function, tetratricopeptide, tetratricopeptide repeat |
| Biological source | SYNTHETIC CONSTRUCT |
| Total number of polymer chains | 3 |
| Total formula weight | 43920.28 |
| Authors | Albrecht, R.,Zhu, H.,Hartmann, M.D. (deposition date: 2016-03-15, release date: 2016-10-12, Last modification date: 2024-05-08) |
| Primary citation | Zhu, H.,Sepulveda, E.,Hartmann, M.D.,Kogenaru, M.,Ursinus, A.,Sulz, E.,Albrecht, R.,Coles, M.,Martin, J.,Lupas, A.N. Origin of a folded repeat protein from an intrinsically disordered ancestor. Elife, 5:-, 2016 Cited by PubMed Abstract: Repetitive proteins are thought to have arisen through the amplification of subdomain-sized peptides. Many of these originated in a non-repetitive context as cofactors of RNA-based replication and catalysis, and required the RNA to assume their active conformation. In search of the origins of one of the most widespread repeat protein families, the tetratricopeptide repeat (TPR), we identified several potential homologs of its repeated helical hairpin in non-repetitive proteins, including the putatively ancient ribosomal protein S20 (RPS20), which only becomes structured in the context of the ribosome. We evaluated the ability of the RPS20 hairpin to form a TPR fold by amplification and obtained structures identical to natural TPRs for variants with 2-5 point mutations per repeat. The mutations were neutral in the parent organism, suggesting that they could have been sampled in the course of evolution. TPRs could thus have plausibly arisen by amplification from an ancestral helical hairpin. PubMed: 27623012DOI: 10.7554/eLife.16761 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.148 Å) |
Structure validation
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