Open AccessStructural and functional insight into the universal stress protein family
Author(s) -
Tkaczuk Karolina L.,
A. Shumilin Igor,
Chruszcz Maksymilian,
Evdokimova Elena,
Savchenko Alexei,
Minor Wladek
Publication year - 2013
Publication title -
evolutionary applications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.776
H-Index - 68
ISSN - 1752-4571
DOI - 10.1111/eva.12057
Subject(s) - biology , structural genomics , context (archaeology) , computational biology , structural similarity , genetics , function (biology) , evolutionary biology , sequence (biology) , similarity (geometry) , protein structure , biochemistry , artificial intelligence , computer science , paleontology , image (mathematics)
We present the crystal structures of two universal stress proteins ( USP ) from A rchaeoglobus fulgidus and N itrosomonas europaea in both apo ‐ and ligand‐bound forms. This work is the first complete synthesis of the structural properties of 26 USP available in the P rotein D ata B ank, over 75% of which were determined by structure genomics centers with no additional information provided. The results of bioinformatic analyses of all available USP structures and their sequence homologs revealed that these two new USP structures share overall structural similarity with structures of USP s previously determined. Clustering and cladogram analyses, however, show how they diverge from other members of the USP superfamily and show greater similarity to USP s from organisms inhabiting extreme environments. We compared them with other archaeal and bacterial USP s and discuss their similarities and differences in context of structure, sequential motifs, and potential function. We also attempted to group all analyzed USP s into families, so that assignment of the potential function to those with no experimental data available would be possible by extrapolation.