Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis.

摘要: With the advent of sequencing programs prokaryotic genomes, many examples presence serine/threonine protein kinases in these organisms have been identified. Moreover, could be classified as homologues those belonging to well characterized superfamily eukaryotic and tyrosine kinases. Eleven such were recognized genome Mycobacterium tuberculosis. Here we report crystal structure an active form PknB, one four M. tuberculosis that are conserved downsized leprae therefore presumed play important role processes regulate complex life cycle mycobacteria. Our confirms again extraordinary conservation kinase fold constitutes a landmark extends this across evolutionary distance between high eukaryotes eubacteria. The with nucleotide triphosphate analog, reveals enzyme state unprecedented arrangement Gly-rich loop associated new conformation γ-phosphoryl group. It presents partially disordered activation loop, suggesting induced fit mode binding for so far unknown substrates or some modulating factor(s).