Download MendeleyTyrosine binding and promiscuity in the arginine repressor from the pathogenic bacterium Corynebacterium pseudotuberculosis.
Mariutti, R.B., Ullah, A., Araujo, G.C., Murakami, M.T., Arni, R.K.(2016) Biochem Biophys Res Commun 475: 350-355
- PubMed: 27233609
- DOI: https://doi.org/10.1016/j.bbrc.2016.05.091
- Primary Citation of Related Structures:
5JVO - PubMed Abstract:
The arginine repressor (ArgR) regulates arginine biosynthesis in a number of microorganisms and consists of two domains interlinked by a short peptide; the N-terminal domain is involved in DNA binding and the C-terminal domain binds arginine and forms a hexamer made-up of a dimer of trimers. The crystal structure of the C-terminal domain of ArgR from the pathogenic Corynebacterium pseudotuberculosis determined at 1.9 Å resolution contains a tightly bound tyrosine at the arginine-binding site indicating hitherto unobserved promiscuity. Structural analysis of the binding pocket displays clear molecular adaptations to accommodate tyrosine binding suggesting the possible existence of an alternative regulatory process in this pathogenic bacterium.
Organizational Affiliation:
Multiuser Center for Biomolecular Innovation, IBILCE/UNESP, São José do Rio Preto, SP, 15054-000, Brazil. Electronic address: mariutti@ibilce.unesp.br.
