7R6O
Pyrrolysyl-tRNA synthetase from methanogenic archaeon ISO4-G1 (G1PylRS)
Summary for 7R6O
| Entry DOI | 10.2210/pdb7r6o/pdb |
| Descriptor | Pyrrolysyl-tRNA synthetase PylS, 1,2-ETHANEDIOL, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | trna synthetases, trna-ligase, trna synthetases class ii, translation |
| Biological source | methanogenic archaeon mixed culture ISO4-G1 |
| Total number of polymer chains | 4 |
| Total formula weight | 123854.60 |
| Authors | Frkic, R.L.,Huber, T.,Jackson, C.J. (deposition date: 2021-06-23, release date: 2022-03-02, Last modification date: 2023-10-18) |
| Primary citation | Abdelkader, E.H.,Qianzhu, H.,George, J.,Frkic, R.L.,Jackson, C.J.,Nitsche, C.,Otting, G.,Huber, T. Genetic Encoding of Cyanopyridylalanine for In-Cell Protein Macrocyclization by the Nitrile-Aminothiol Click Reaction. Angew.Chem.Int.Ed.Engl., 61:e202114154-e202114154, 2022 Cited by PubMed Abstract: Cyanopyridylalanines are non-canonical amino acids that react with aminothiol compounds under physiological conditions in a biocompatible manner without requiring added catalyst. Here we present newly developed aminoacyl-tRNA synthetases for genetic encoding of meta- and para-cyanopyridylalanine to enable the site-specific attachment of a wide range of different functionalities. The outstanding utility of the cyanopyridine moiety is demonstrated by examples of i) post-translational functionalization of proteins, ii) in-cell macrocyclization of peptides and proteins, and iii) protein stapling. The biocompatible nature of the protein ligation chemistry enabled by the cyanopyridylalanine amino acid opens a new path to specific in vivo protein modifications in complex biological environments. PubMed: 35102680DOI: 10.1002/anie.202114154 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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