1TFO

Ribonuclease from Escherichia coli complexed with its inhibitor protein

1TFO の概要

• エントリーDOI: 10.2210/pdb1tfo/pdb
• 関連するPDBエントリー: 1TFK
• 分子名称: Colicin D, Colicin D immunity protein (3 entities in total)
• 機能のキーワード: protein-protein complex, toxin-toxin inhibitor complex, toxin/toxin inhibitor
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22512.56

構造登録者

Yajima, S.,Nakanishi, K.,Takahashi, K.,Ogawa, T.,Kezuka, Y.,Hidaka, M.,Nonaka, T.,Ohsawa, K.,Masaki, H. (登録日: 2004-05-27, 公開日: 2005-03-01, 最終更新日: 2024-02-14)

主引用文献

Yajima, S.,Nakanishi, K.,Takahashi, K.,Ogawa, T.,Hidaka, M.,Kezuka, Y.,Nonaka, T.,Ohsawa, K.,Masaki, H.
Relation between tRNase activity and the structure of colicin D according to X-ray crystallography
Biochem.Biophys.Res.Commun., 322:966-973, 2004

PubMed Abstract: Colicin D is a plasmid-encoded proteinaceous toxin which kills sensitive Escherichia coli. Toxicity stems from ribonuclease activity that targets exclusively four isoacceptors of tRNA(Arg) with a cleavage position between 38 and 39 of the corresponding anticodons. Since no other tRNAs with the same sequences at 38 and 39 as tRNA(Arg)s are cleaved, colicin D should be capable of recognizing some higher order structure of tRNAs. We report here two crystal structures of catalytic domains of colicin D which have different N-terminal lengths, both complexed with its cognate inhibitor protein, ImmD. A row of positive charge patches is found on the surface of the catalytic domain, suggestive of the binding site of the tRNAs. This finding, together with our refined tRNase activity experiments, indicates that the catalytic domain starting at position 595 has activity almost equivalent to that of colicin D.

PubMed: 15336558
DOI: 10.1016/j.bbrc.2004.07.206

実験手法

X-RAY DIFFRACTION (2.3 Å)