Conformational itinerary of pseudomonas aeruginosa 1,6-anhydro-N- acetylmuramic acid kinase during its catalytic cycle

Abstract

Background: AnmK is an unusual sugar kinase that both cleaves and phosphorylates its 1,6-anhMurNAc substrate. Results: Crystallographic and solution x-ray scattering analyses demonstrate significant conformational rearrangements of AnmK during catalysis. Conclusion: Ligand binding at the active site of AnmK coordinates its conformational itinerary. Significance: The unique dual activities of AnmK coupled with its complex structural dynamics advance our understanding of the diverse reactions carried out by sugar kinases. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc..