Elevated μs-ms timescale backbone dynamics in the transition state analog form of arginine kinase.

ABSTRACT: Arginine kinase catalyzes reversible phosphoryl transfer between arginine and ATP. Crystal structures of arginine kinase in an open, substrate-free form and closed, transition state analog (TSA) complex indicate that the enzyme undergoes substantial domain and loop rearrangements required for substrate binding, catalysis, and product release. Nuclear magnetic resonance (NMR) has shown that substrate-free arginine kinase is rigid on the ps-ns timescale (average S²=0.84±0.08) yet quite dynamic on the µs-ms timescale (35 residues with R_ex, 12%), and that movements of the N-terminal domain and the loop comprising residues I182-G209 are rate-limiting on catalysis. Here, NMR of the TSA-bound enzyme shows similar rigidity on the ps-ns timescale (average S²=0.91±0.

SUBMITTER: Davulcu O 

PROVIDER: S-EPMC5677571 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature