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

The Journal of Biological Chemistry
John-Paul BacikBrian L Mark

Abstract

Anhydro-sugar kinases are unique from other sugar kinases in that they must cleave the 1,6-anhydro ring of their sugar substrate to phosphorylate it using ATP. Here we show that the peptidoglycan recycling enzyme 1,6-anhydro-N-acetylmuramic acid kinase (AnmK) from Pseudomonas aeruginosa undergoes large conformational changes during its catalytic cycle, with its two domains rotating apart by up to 32° around two hinge regions to expose an active site cleft into which the substrates 1,6-anhydroMurNAc and ATP can bind. X-ray structures of the open state bound to a nonhydrolyzable ATP analog (AMPPCP) and 1,6-anhydroMurNAc provide detailed insight into a ternary complex that forms preceding an operative Michaelis complex. Structural analysis of the hinge regions demonstrates a role for nucleotide binding and possible cross-talk between the bound ligands to modulate the opening and closing of AnmK. Although AnmK was found to exhibit similar binding affinities for ATP, ADP, and AMPPCP according to fluorescence spectroscopy, small angle x-ray scattering analyses revealed that AnmK adopts an open conformation in solution in the absence of ligand and that it remains in this open state after binding AMPPCP, as we had observed for our crys...Continue Reading

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Citations

May 17, 2015·Journal of Theoretical Biology·Jianghong DaiHongxun Zhang
Jul 16, 2016·IUBMB Life·John-Paul Bacik, Laura R Jarboe
Dec 19, 2017·Chembiochem : a European Journal of Chemical Biology·Christina RotherBernd Nidetzky
Sep 12, 2015·The Journal of Biological Chemistry·John-Paul BacikRyszard Michalczyk
May 31, 2018·Chemical Reviews·David A DikShahriar Mobashery

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