A conserved P-loop anchor limits the structural dynamics that mediate nucleotide dissociation in EF-Tu.

ABSTRACT: The phosphate-binding loop (P-loop) is a conserved sequence motif found in mononucleotide-binding proteins. Little is known about the structural dynamics of this region and its contribution to the observed nucleotide binding properties. Understanding the underlying design principles is of great interest for biomolecular engineering applications. We have used rapid-kinetics measurements in vitro and molecular dynamics (MD) simulations in silico to investigate the relationship between GTP-binding properties and P-loop structural dynamics in the universally conserved Elongation Factor (EF) Tu. Analysis of wild type EF-Tu and variants with substitutions at positions in or adjacent to the P-loop revealed a correlation between P-loop flexibility and the entropy of activation for GTP dissociation

SUBMITTER: Mercier E 

PROVIDER: S-EPMC4286738 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature