6ZI0

Crystal structure of the isolated H. influenzae VapD toxin (wildtype)

これはPDB形式変換不可エントリーです。

6ZI0 の概要

• エントリーDOI: 10.2210/pdb6zi0/pdb
• 分子名称: Endoribonuclease VapD (2 entities in total)
• 機能のキーワード: toxin-antitoxin, vapxd, rnase, nucleic-acid binding protein, hydrolase, toxin
• 由来する生物種: Haemophilus influenzae 86-028NP
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11870.34

構造登録者

Bertelsen, M.B.,Senissar, M.,Nielsen, M.H.,Bisiak, F.,Cunha, M.V.,Molinaro, A.L.,Daines, D.A.,Brodersen, D.E. (登録日: 2020-06-24, 公開日: 2020-10-14, 最終更新日: 2024-01-31)

主引用文献

Bertelsen, M.B.,Senissar, M.,Nielsen, M.H.,Bisiak, F.,Cunha, M.V.,Molinaro, A.L.,Daines, D.A.,Brodersen, D.E.
Structural Basis for Toxin Inhibition in the VapXD Toxin-Antitoxin System.
Structure, 29:139-, 2021

PubMed Abstract: Bacterial type II toxin-antitoxin (TA) modules encode a toxic protein that downregulates metabolism and a specific antitoxin that binds and inhibits the toxin during normal growth. In non-typeable Haemophilus influenzae, a common cause of infections in humans, the vapXD locus was found to constitute a functional TA module and contribute to pathogenicity; however, the mode of action of VapD and the mechanism of inhibition by the VapX antitoxin remain unknown. Here, we report the structure of the intact H. influenzae VapXD complex, revealing an unusual 2:1 TA molecular stoichiometry where a Cas2-like homodimer of VapD binds a single VapX antitoxin. VapX consists of an oligonucleotide/oligosaccharide-binding domain that docks into an asymmetrical cavity on the toxin dimer. Structures of isolated VapD further reveal how a symmetrical toxin homodimer adapts to interacting with an asymmetrical antitoxin and suggest how a primordial TA system evolved to become part of CRISPR-Cas immunity systems.

PubMed: 33096014
DOI: 10.1016/j.str.2020.10.002

実験手法

X-RAY DIFFRACTION (2.5 Å)