Tyrosine binding and promiscuity in the arginine repressor from the pathogenic bacterium Corynebacterium pseudotuberculosis
Arquivos
Data
2016-07-08
Autores
Mariutti, Ricardo Barros [UNESP]
Ullah, Anwar [UNESP]
Araujo, Gabriela Campos [UNESP]
Murakami, Mario Tyago
Arni, Raghuvir Krishnaswamy [UNESP]
Título da Revista
ISSN da Revista
Título de Volume
Editor
Resumo
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.
Descrição
Palavras-chave
Arginine repressor, Corynebacterium pseudotuberculosis, Crystal structure, Promiscuity, Tyrosine
Como citar
Biochemical and Biophysical Research Communications, v. 475, n. 4, p. 350-355, 2016.