5JVO

Crystal structure of the Arginine Repressor from the pathogenic bacterium Corynebacterium pseudotuberculosis

Summary for 5JVO

• Entry DOI: 10.2210/pdb5jvo/pdb
• Descriptor: Arginine repressor, TYROSINE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: arginine repressor, dna binding protein
• Biological source: Corynebacterium pseudotuberculosis
• Cellular location: Cytoplasm : A0A0E3UAP8
• Total number of polymer chains: 2
• Total formula weight: 21726.26

Authors

Mariutti, R.B.,Ullah, A.,Murakami, M.T.,Arni, R.K. (deposition date: 2016-05-11, release date: 2016-08-31, Last modification date: 2023-09-27)

Primary citation

Mariutti, R.B.,Ullah, A.,Araujo, G.C.,Murakami, M.T.,Arni, R.K.
Tyrosine binding and promiscuity in the arginine repressor from the pathogenic bacterium Corynebacterium pseudotuberculosis.
Biochem.Biophys.Res.Commun., 475:350-355, 2016

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.

PubMed: 27233609
DOI: 10.1016/j.bbrc.2016.05.091

Experimental method

X-RAY DIFFRACTION (1.9 Å)