5V59
Crystal structure of catalytic fragment of human AlaRS in complex with Aze-SA
Summary for 5V59
| Entry DOI | 10.2210/pdb5v59/pdb |
| Related | 5V58 |
| Descriptor | Alanine--tRNA ligase, cytoplasmic, 5'-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine (3 entities in total) |
| Functional Keywords | ligase, aminoacyl-trna synthetase, non-proteinogenic amino acid |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 53743.60 |
| Authors | Zhou, H.,Song, Y.,Schimmel, P. (deposition date: 2017-03-13, release date: 2018-01-10, Last modification date: 2023-10-04) |
| Primary citation | Song, Y.,Zhou, H.,Vo, M.N.,Shi, Y.,Nawaz, M.H.,Vargas-Rodriguez, O.,Diedrich, J.K.,Yates, J.R.,Kishi, S.,Musier-Forsyth, K.,Schimmel, P. Double mimicry evades tRNA synthetase editing by toxic vegetable-sourced non-proteinogenic amino acid. Nat Commun, 8:2281-2281, 2017 Cited by PubMed Abstract: Hundreds of non-proteinogenic (np) amino acids (AA) are found in plants and can in principle enter human protein synthesis through foods. While aminoacyl-tRNA synthetase (AARS) editing potentially provides a mechanism to reject np AAs, some have pathological associations. Co-crystal structures show that vegetable-sourced azetidine-2-carboxylic acid (Aze), a dual mimic of proline and alanine, is activated by both human prolyl- and alanyl-tRNA synthetases. However, it inserts into proteins as proline, with toxic consequences in vivo. Thus, dual mimicry increases odds for mistranslation through evasion of one but not both tRNA synthetase editing systems. PubMed: 29273753DOI: 10.1038/s41467-017-02201-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.03 Å) |
Structure validation
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