2AN7

Solution structure of the bacterial antidote ParD

2AN7 の概要

• エントリーDOI: 10.2210/pdb2an7/pdb
• NMR情報: BMRB: 4792
• 分子名称: Protein parD (1 entity in total)
• 機能のキーワード: bacterial antidote, ribbon-helix-helix, dna-binding motif, plasmid addiction, dna binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18228.50

構造登録者

Oberer, M.,Zangger, K.,Gruber, K.,Keller, W. (登録日: 2005-08-11, 公開日: 2006-09-05, 最終更新日: 2024-05-15)

主引用文献

Oberer, M.,Zangger, K.,Gruber, K.,Keller, W.
The solution structure of ParD, the antidote of the ParDE toxin antitoxin module, provides the structural basis for DNA and toxin binding.
Protein Sci., 16:1676-1688, 2007

PubMed Abstract: ParD is the antidote of the plasmid-encoded toxin-antitoxin (TA) system ParD-ParE. These modules rely on differential stabilities of a highly expressed but labile antidote and a stable toxin expressed from one operon. Consequently, loss of the coding plasmid results in loss of the protective antidote and poisoning of the cell. The antidote protein usually also exhibits an autoregulatory function of the operon. In this paper, we present the solution structure of ParD. The repressor activity of ParD is mediated by the N-terminal half of the protein, which adopts a ribbon-helix-helix (RHH) fold. The C-terminal half of the protein is unstructured in the absence of its cognate binding partner ParE. Based on homology with other RHH proteins, we present a model of the ParD-DNA interaction, with the antiparallel beta-strand being inserted into the major groove of DNA. The fusion of the N-terminal DNA-binding RHH motif to the toxin-binding unstructured C-terminal domain is discussed in its evolutionary context.

PubMed: 17656583
DOI: 10.1110/ps.062680707

実験手法

SOLUTION NMR