3G98

Crystal Structure of the C-Ala domain from Aquifex aeolicus alanyl-tRNA synthetase

3G98 の概要

• エントリーDOI: 10.2210/pdb3g98/pdb
• 分子名称: Alanyl-tRNA synthetase (2 entities in total)
• 機能のキーワード: alpha and beta fold, aminoacyl-trna synthetase, atp-binding, cytoplasm, ligase, nucleotide-binding, protein biosynthesis
• 由来する生物種: Aquifex aeolicus
• 細胞内の位置: Cytoplasm: O67323
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24323.99

構造登録者

Guo, M.,Yang, X.L.,Schimmel, P. (登録日: 2009-02-13, 公開日: 2009-10-06, 最終更新日: 2024-02-21)

主引用文献

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

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: 19661429
DOI: 10.1126/science.1174343

実験手法

X-RAY DIFFRACTION (1.85 Å)