research data . Dataset . 2016

Functional Sites Induce Long-Range Evolutionary Constraints in Enzymes

Jack, Benjamin R.; G. Meyer, Austin; Echave, Julian; O. Wilke, Claus;
  • Published: 01 Jan 2016
  • Publisher: Figshare
Abstract
<div><p>Functional residues in proteins tend to be highly conserved over evolutionary time. However, to what extent functional sites impose evolutionary constraints on nearby or even more distant residues is not known. Here, we report pervasive conservation gradients toward catalytic residues in a dataset of 524 distinct enzymes: evolutionary conservation decreases approximately linearly with increasing distance to the nearest catalytic residue in the protein structure. This trend encompasses, on average, 80% of the residues in any enzyme, and it is independent of known structural constraints on protein evolution such as residue packing or solvent accessibility....
Subjects
free text keywords: Biophysics, Biochemistry, Evolutionary Biology, Cancer, 110309 Infectious Diseases, 69999 Biological Sciences not elsewhere classified, 29999 Physical Sciences not elsewhere classified, site, multimeric enzymes, protein structure, rate gradients, observations show, protein evolution, enzyme size, enzyme structure, conservation decreases, Enzymes Functional residues, constraint, conservation gradients
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Dataset . 2016
Provider: figshare
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