Investigation of the Relationship between the S1 Domain and Its Molecular Functions Derived from Studies of the Tertiary Structure
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...
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doaj-77b8fd079c4e4a879b707fbf192b89b22020-11-25T02:22:58ZengMDPI AGMolecules1420-30492019-10-012420368110.3390/molecules24203681molecules24203681Investigation of the Relationship between the S1 Domain and Its Molecular Functions Derived from Studies of the Tertiary StructureEvgenia I. Deryusheva0Andrey V. Machulin1Maxim A. Matyunin2Oxana V. Galzitskaya3Institute for Biological Instrumentation, Federal Research Center “Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences”, 142290 Pushchino, Moscow Region, RussiaSkryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Federal Research Center “Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences”, 142290 Pushchino, Moscow Region, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, RussiaS1 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.https://www.mdpi.com/1420-3049/24/20/3681s1 domainrna-bindingstructural repeats30 s ribosomal protein s1 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Evgenia I. Deryusheva Andrey V. Machulin Maxim A. Matyunin Oxana V. Galzitskaya |
spellingShingle |
Evgenia I. Deryusheva Andrey V. Machulin Maxim A. Matyunin Oxana V. Galzitskaya Investigation of the Relationship between the S1 Domain and Its Molecular Functions Derived from Studies of the Tertiary Structure Molecules s1 domain rna-binding structural repeats 30 s ribosomal protein s1 |
author_facet |
Evgenia I. Deryusheva Andrey V. Machulin Maxim A. Matyunin Oxana V. Galzitskaya |
author_sort |
Evgenia I. Deryusheva |
title |
Investigation of the Relationship between the S1 Domain and Its Molecular Functions Derived from Studies of the Tertiary Structure |
title_short |
Investigation of the Relationship between the S1 Domain and Its Molecular Functions Derived from Studies of the Tertiary Structure |
title_full |
Investigation of the Relationship between the S1 Domain and Its Molecular Functions Derived from Studies of the Tertiary Structure |
title_fullStr |
Investigation of the Relationship between the S1 Domain and Its Molecular Functions Derived from Studies of the Tertiary Structure |
title_full_unstemmed |
Investigation of the Relationship between the S1 Domain and Its Molecular Functions Derived from Studies of the Tertiary Structure |
title_sort |
investigation of the relationship between the s1 domain and its molecular functions derived from studies of the tertiary structure |
publisher |
MDPI AG |
series |
Molecules |
issn |
1420-3049 |
publishDate |
2019-10-01 |
description |
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. |
topic |
s1 domain rna-binding structural repeats 30 s ribosomal protein s1 |
url |
https://www.mdpi.com/1420-3049/24/20/3681 |
work_keys_str_mv |
AT evgeniaideryusheva investigationoftherelationshipbetweenthes1domainanditsmolecularfunctionsderivedfromstudiesofthetertiarystructure AT andreyvmachulin investigationoftherelationshipbetweenthes1domainanditsmolecularfunctionsderivedfromstudiesofthetertiarystructure AT maximamatyunin investigationoftherelationshipbetweenthes1domainanditsmolecularfunctionsderivedfromstudiesofthetertiarystructure AT oxanavgalzitskaya investigationoftherelationshipbetweenthes1domainanditsmolecularfunctionsderivedfromstudiesofthetertiarystructure |
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