title: Tyrosine binding and promiscuity in the arginine repressor from the pathogenic bacterium Corynebacterium pseudotuberculosis.
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.
authors.affiliation: Multiuser Center for Biomolecular Innovation, IBILCE/UNESP, São José do Rio Preto, SP, 15054-000, Brazil. Electronic address: mariutti@ibilce.unesp.br.
authors.forename: Ricardo Barros
authors.initials: RB
authors.lastname: Mariutti
authors.affiliation: Multiuser Center for Biomolecular Innovation, IBILCE/UNESP, São José do Rio Preto, SP, 15054-000, Brazil; Department of Biosciences, COMSATS Institute of Information Technology, Park Road, Islamabad 45550, Pakistan.
authors.forename: Anwar
authors.initials: A
authors.lastname: Ullah
authors.affiliation: Department of Physics, IBILCE/UNESP, São José do Rio Preto, SP, 15054-000, Brazil.
authors.forename: Gabriela Campos
authors.initials: GC
authors.lastname: Araujo
authors.affiliation: Biosciences National Laboratory (LNBio), National Center for Research in Energy and Materials (CNPEM), Campinas, São Paulo, 13083-100, Brazil.
authors.forename: Mario Tyago
authors.initials: MT
authors.lastname: Murakami
authors.affiliation: Multiuser Center for Biomolecular Innovation, IBILCE/UNESP, São José do Rio Preto, SP, 15054-000, Brazil; Department of Physics, IBILCE/UNESP, São José do Rio Preto, SP, 15054-000, Brazil. Electronic address: arni@sjrp.unesp.br.
authors.forename: Raghuvir Krishnaswamy
authors.initials: RK
authors.lastname: Arni
mesh_terms: D000595:Amino Acid Sequence; D001120:Arginine / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D003354:Corynebacterium Infections / Q000382:microbiology; D016925:Corynebacterium pseudotuberculosis / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D000072417:Protein Domains; D012097:Repressor Proteins / Q000737:chemistry* / Q000378:metabolism; D013379:Substrate Specificity; D014443:Tyrosine / Q000378:metabolism
chemical_list: C087018:ArgR protein, Bacteria; D001426:Bacterial Proteins; D012097:Repressor Proteins; D014443:Tyrosine; D001120:Arginine
keywords: Arginine repressor; Corynebacterium pseudotuberculosis; Crystal structure; Promiscuity; Tyrosine