Investigation of the Relationship between the S1 Domain and Its Molecular Functions Derived from Studies of the Tertiary Structure.
30 S ribosomal protein S1
RNA-binding
S1 domain
structural repeats
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
13 Oct 2019
13 Oct 2019
Historique:
received:
29
09
2019
accepted:
11
10
2019
entrez:
17
10
2019
pubmed:
17
10
2019
medline:
19
2
2020
Statut:
epublish
Résumé
S1 domain, a structural variant of one of the "oldest" OB-folds (oligonucleotide/oligosaccharide-binding fold), is widespread in various proteins in three domains of life: Bacteria, Eukaryotes, and Archaea. In this study, it was shown that S1 domains of bacterial, eukaryotic, and archaeal proteins have a low percentage of identity, which indicates the uniqueness of the scaffold and is associated with protein functions. Assessment of the predisposition of tertiary flexibility of S1 domains using computational and statistical tools showed similar structural features and revealed functional flexible regions that are potentially involved in the interaction of natural binding partners. In addition, we analyzed the relative number and distribution of S1 domains in all domains of life and established specific features based on sequences and structures associated with molecular functions. The results correlate with the presence of repeats of the S1 domain in proteins containing the S1 domain in the range from one (bacterial and archaeal) to 15 (eukaryotic) and, apparently, are associated with the need for individual proteins to increase the affinity and specificity of protein binding to ligands.
Identifiants
pubmed: 31614904
pii: molecules24203681
doi: 10.3390/molecules24203681
pmc: PMC6832287
pii:
doi:
Substances chimiques
Archaeal Proteins
0
Bacterial Proteins
0
Oligonucleotides
0
Oligosaccharides
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Russian Science Foundation
ID : 18-14-00321
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