5IFG

Crystal structure of HigA-HigB complex from E. Coli

5IFG の概要

• エントリーDOI: 10.2210/pdb5ifg/pdb
• 分子名称: mRNA interferase HigB, Antitoxin HigA (2 entities in total)
• 機能のキーワード: mrna interferase, hydrolase-antitoxin complex, hydrolase/antitoxin
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 55019.30

構造登録者

Yang, J.S.,Zhou, K.,Gao, z.Q.,Liu, Q.S.,Dong, Y.H. (登録日: 2016-02-26, 公開日: 2017-03-01, 最終更新日: 2024-10-16)

主引用文献

Yang, J.,Zhou, K.,Liu, P.,Dong, Y.,Gao, Z.,Zhang, J.,Liu, Q.
Structural insight into the E. coli HigBA complex
Biochem. Biophys. Res. Commun., 478:1521-1527, 2016

PubMed Abstract: The toxin-antitoxin system is ubiquitously existed in bacteria and archaea, performing a wide variety of functions modulating cell fitness in response to environmental cues. In this report, we solved the crystal structure of the toxin-antitoxin HigBA complex from E. coli K-12 to 2.7 Å resolution. The crystal structure of the HigBA complex displays a hetero-tetramer (HigBA)2 form comprised by two HigB and two HigA subunits. Each toxin HigB resumes a microbial RNase T1 fold, characteristic of a three antiparallel β-sheet core shielded by a few α-helices at either side. Each antitoxin HigA composed of all α-helices resembles a "C"-shaped clamp nicely encompassing a HigB in the (HigBA)2 complex. Two HigA monomers dimerize at their N-terminal domain. We showed that HigA helix α1 was essential for HigA dimerization and the hetero-tetramer (HigBA)2 formation, but not for a hetero-dimeric HigBA formation. HigA dimerization mediated by helix α1 was dispensable for DNA-binding, as a heterodimeric HigBA complex still bound to the higBA operator in vitro. The HigA C-terminal domain with a helix-turn-helix fold was essential for DNA binding. We also defined two palindromes in higBA operator specifically recognized by HigA and HigBA in vitro.

PubMed: 27601326
DOI: 10.1016/j.bbrc.2016.08.131

実験手法

X-RAY DIFFRACTION (2.702 Å)