4O87

Crystal structure of a N-tagged Nuclease

4O87 の概要

• エントリーDOI: 10.2210/pdb4o87/pdb
• 関連するPDBエントリー: 4O88
• 分子名称: N-tagged Nuclease, CITRIC ACID, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: novel fold, nuclease, hydrolase
• 由来する生物種: Millerozyma acaciae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75597.60

構造登録者

Chakravarty, A.K.,Smith, P.,Shuman, S. (登録日: 2013-12-26, 公開日: 2014-10-15, 最終更新日: 2024-02-28)

主引用文献

Chakravarty, A.K.,Smith, P.,Jalan, R.,Shuman, S.
Structure, mechanism, and specificity of a eukaryal tRNA restriction enzyme involved in self-nonself discrimination.
Cell Rep, 7:339-347, 2014

PubMed Abstract: tRNA restriction by anticodon nucleases underlies cellular stress responses and self-nonself discrimination in a wide range of taxa. Anticodon breakage inhibits protein synthesis, which, in turn, results in growth arrest or cell death. The eukaryal ribotoxin PaT secreted by Pichia acaciae inhibits growth of Saccharomyces cerevisiae via cleavage of tRNA(Gln(UUG)). We find that recombinant PaT incises a synthetic tRNA(Gln(UUG)) stem-loop RNA by transesterification at a single site 3' of the wobble uridine, yielding 2',3'-cyclic phosphate and 5'-OH ends. Incision is suppressed by replacement of the wobble nucleobase with adenine or guanine. The crystal structure of PaT reveals a distinctive fold and active site, essential components of which are demonstrated by mutagenesis. Pichia acaciae evades self-toxicity via a distinctive intracellular immunity protein, ImmPaT, which binds PaT and blocks nuclease activity. Our results highlight the evolutionary diversity of tRNA restriction and immunity systems.

PubMed: 24726365
DOI: 10.1016/j.celrep.2014.03.034

実験手法

X-RAY DIFFRACTION (1.8 Å)