1WMI

Crystal structure of archaeal RelE-RelB complex from Pyrococcus horikoshii OT3

1WMI の概要

• エントリーDOI: 10.2210/pdb1wmi/pdb
• 分子名称: hypothetical protein PHS013, hypothetical protein PHS014 (3 entities in total)
• 機能のキーワード: toxin-antitoxin complex, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Pyrococcus horikoshii; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 37815.62

構造登録者

Takagi, H.,Kakuta, Y.,Kamachi, R.,Yao, M.,Tanaka, I.,Kimura, M. (登録日: 2004-07-09, 公開日: 2005-03-15, 最終更新日: 2024-03-13)

主引用文献

Takagi, H.,Kakuta, Y.,Okada, T.,Yao, M.,Tanaka, I.,Kimura, M.
Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects
Nat.Struct.Mol.Biol., 12:327-331, 2005

PubMed Abstract: The Escherichia coli chromosome encodes toxin-antitoxin pairs. The toxin RelE cleaves mRNA positioned at the A-site in ribosomes, whereas the antitoxin RelB relieves the effect of RelE. The hyperthermophilic archaeon Pyrococcus horikoshii OT3 has the archaeal homologs aRelE and aRelB. Here we report the crystal structure of aRelE in complex with aRelB determined at a resolution of 2.3 A. aRelE folds into an alpha/beta structure, whereas aRelB lacks a distinct hydrophobic core and extensively wraps around the molecular surface of aRelE. Neither component shows structural homology to known ribonucleases or their inhibitors. Site-directed mutagenesis suggests that Arg85, in the C-terminal region, is strongly involved in the functional activity of aRelE, whereas Arg40, Leu48, Arg58 and Arg65 play a modest role in the toxin's activity.

PubMed: 15768033
DOI: 10.1038/nsmb911

実験手法

X-RAY DIFFRACTION (2.3 Å)