3G98
Crystal Structure of the C-Ala domain from Aquifex aeolicus alanyl-tRNA synthetase
Summary for 3G98
| Entry DOI | 10.2210/pdb3g98/pdb |
| Descriptor | Alanyl-tRNA synthetase (2 entities in total) |
| Functional Keywords | alpha and beta fold, aminoacyl-trna synthetase, atp-binding, cytoplasm, ligase, nucleotide-binding, protein biosynthesis |
| Biological source | Aquifex aeolicus |
| Cellular location | Cytoplasm: O67323 |
| Total number of polymer chains | 2 |
| Total formula weight | 24323.99 |
| Authors | Guo, M.,Yang, X.L.,Schimmel, P. (deposition date: 2009-02-13, release date: 2009-10-06, Last modification date: 2024-02-21) |
| Primary citation | Guo, M.,Chong, Y.E.,Beebe, K.,Shapiro, R.,Yang, X.L.,Schimmel, P. The C-Ala domain brings together editing and aminoacylation functions on one tRNA. Science, 325:744-747, 2009 Cited by PubMed Abstract: Protein synthesis involves the accurate attachment of amino acids to their matching transfer RNA (tRNA) molecules. Mistranslating the amino acids serine or glycine for alanine is prevented by the function of independent but collaborative aminoacylation and editing domains of alanyl-tRNA synthetases (AlaRSs). We show that the C-Ala domain plays a key role in AlaRS function. The C-Ala domain is universally tethered to the editing domain both in AlaRS and in many homologous free-standing editing proteins. Crystal structure and functional analyses showed that C-Ala forms an ancient single-stranded nucleic acid binding motif that promotes cooperative binding of both aminoacylation and editing domains to tRNA(Ala). In addition, C-Ala may have played an essential role in the evolution of AlaRSs by coupling aminoacylation to editing to prevent mistranslation. PubMed: 19661429DOI: 10.1126/science.1174343 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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