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3BS1

Structure of the Staphylococcus aureus AgrA LytTR Domain Bound to DNA Reveals a Beta Fold with a Novel Mode of Binding

3BS1 の概要
エントリーDOI10.2210/pdb3bs1/pdb
分子名称DNA (5'-D(*DTP*DTP*DTP*DAP*DAP*DCP*DAP*DGP*DTP*DTP*DAP*DAP*DGP*(BRU)P*DAP*DT)-3'), DNA (5'-D(*DAP*DAP*(BRU)P*DAP*DCP*DTP*DTP*DAP*DAP*DCP*DTP*DGP*DTP*DTP*DAP*DA)-3'), Accessory gene regulator protein A, ... (5 entities in total)
機能のキーワードlyttr, agra, response regulator, dna binding domain, activator, cytoplasm, dna-binding, phosphoprotein, transcription, transcription regulation, two-component regulatory system, transcription regulator
由来する生物種Staphylococcus aureus
詳細
細胞内の位置Cytoplasm: 3BS1
タンパク質・核酸の鎖数3
化学式量合計22327.71
構造登録者
Sidote, D.J.,Barbieri, C.,Wu, T.,Stock, A.M. (登録日: 2007-12-21, 公開日: 2008-04-08, 最終更新日: 2024-02-21)
主引用文献Sidote, D.J.,Barbieri, C.M.,Wu, T.,Stock, A.M.
Structure of the Staphylococcus aureus AgrA LytTR Domain Bound to DNA Reveals a Beta Fold with an Unusual Mode of Binding.
Structure, 16:727-735, 2008
Cited by
PubMed Abstract: The LytTR domain is a DNA-binding motif found within the AlgR/AgrA/LytR family of transcription factors that regulate virulence factor and toxin gene expression in pathogenic bacteria. This previously uncharacterized domain lacks sequence similarity with proteins of known structure. The crystal structure of the DNA-binding domain of Staphylococcus aureus AgrA complexed with a DNA pentadecamer duplex has been determined at 1.6 A resolution. The structure establishes a 10-stranded beta fold for the LytTR domain and reveals its mode of interaction with DNA. Residues within loop regions of AgrA contact two successive major grooves and the intervening minor groove on one face of the oligonucleotide duplex, inducing a substantial bend in the DNA. Loss of DNA binding upon substitution of key interacting residues in AgrA supports the observed binding mode. This mode of protein-DNA interaction provides a potential target for future antimicrobial drug design.
PubMed: 18462677
DOI: 10.1016/j.str.2008.02.011
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.6 Å)
構造検証レポート
Validation report summary of 3bs1
検証レポート(詳細版)ダウンロードをダウンロード

248636

件を2026-02-04に公開中

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