Characterizing the relation of functional and Early Folding Residues in protein structures using the example of aminoacyl-tRNA synthetases.

ABSTRACT: Proteins are chains of amino acids which adopt a three-dimensional structure and are then able to catalyze chemical reactions or propagate signals in organisms. Without external influence, many proteins fold into their native structure, and a small number of Early Folding Residues (EFR) have previously been shown to initiate the formation of secondary structure elements and guide their respective assembly. Using the two diverse superfamilies of aminoacyl-tRNA synthetases (aaRS), it is shown that the position of EFR is preserved over the course of evolution even when the corresponding sequence conservation is small. Folding initiation sites are positioned in the center of secondary structure elements, independent of aaRS class. In class I, the predicted position of EFR resembles an ancient

SUBMITTER: Bittrich S 

PROVIDER: S-EPMC6207335 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature