Analysis of the interaction of the nucleotide base with myosin and the effect on substrate efficacy.

ABSTRACT: A wide variety of purine- and pyrimidine-based nucleotides can serve as a substrate for actomyosin mechanics, but with varying effectiveness. To understand the myosin-ATP interaction and in particular, the interactions with the base, we have used molecular dynamics simulations to model the interactions of myosin with ATP, CTP, UTP, aza-ATP, ITP, and GTP (in decreasing order of effectiveness as a substrate for the generation of motility) docked at the active site. The simulations with ATP, and x-ray structures, show a triad of conserved amino acids lining the nucleotide site that form a cyclical chain of nucleotide-protein hydrogen bonding interactions: ATP --> Y135 --> Y116 --> N188 --> ATP. Mechanical efficacy of a substrate correlates with its ability to maintain this coordination. Simul

SUBMITTER: Hyatt D 

PROVIDER: S-EPMC2756361 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature