3bs1
From Proteopedia
Structure of the Staphylococcus aureus AgrA LytTR Domain Bound to DNA Reveals a Beta Fold with a Novel Mode of Binding
Overview
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.
About this Structure
3BS1 is a Protein complex structure of sequences from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
Structure of the Staphylococcus aureus AgrA LytTR Domain Bound to DNA Reveals a Beta Fold with an Unusual Mode of Binding., Sidote DJ, Barbieri CM, Wu T, Stock AM, Structure. 2008 May;16(5):727-35. PMID:18462677 Page seeded by OCA on Thu May 22 22:35:55 2008
Categories: Protein complex | Staphylococcus aureus | Barbieri, C. | Sidote, D J. | Stock, A M. | Wu, T. | Activator | Agra | Cytoplasm | Dna binding domain | Dna-binding | Lyttr | Phosphoprotein | Response regulator | Transcription | Transcription regulation | Transcription regulator | Two-component regulatory system
