Tetrameric Structures of Inorganic CBS-Pyrophosphatases from Various Bacterial Species Revealed by Small-Angle X-ray Scattering in Solution
Quaternary structure of CBS-pyrophosphatases (CBS-PPases), which belong to the PPases of family II, plays an important role in their function ensuring cooperative behavior of the enzymes. Despite an intensive research, high resolution structures of the full-length CBS-PPases are not yet available ma...
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| Format: | Article |
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MDPI AG
2020-04-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/10/4/564 |
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| author | Liubov A. Dadinova Ekaterina Yu. Soshinskaia Cy M. Jeffries Dmitri I. Svergun Eleonora V. Shtykova |
| author_facet | Liubov A. Dadinova Ekaterina Yu. Soshinskaia Cy M. Jeffries Dmitri I. Svergun Eleonora V. Shtykova |
| author_sort | Liubov A. Dadinova |
| collection | DOAJ |
| description | Quaternary structure of CBS-pyrophosphatases (CBS-PPases), which belong to the PPases of family II, plays an important role in their function ensuring cooperative behavior of the enzymes. Despite an intensive research, high resolution structures of the full-length CBS-PPases are not yet available making it difficult to determine the signal transmission path from the regulatory to the active center. In the present work, small-angle X-ray scattering (SAXS) combined with size-exclusion chromatography was applied to determine the solution structures of the full-length wild-type CBS-PPases from three different bacterial species. Previously, in the absence of an experimentally determined full-length CBS-PPase structure, a homodimeric model of the enzyme based on known crystal structures of the CBS domain and family II PPase without this domain has been proposed. Our SAXS analyses demonstrate, for the first time, the existence of stable tetramers in solution for all studied CBS-PPases from different sources. Our findings show that further studies are required to establish the functional properties of these enzymes. This is important not only to enhance our understanding of the relation between CBS-PPases structure and function under normal conditions but also because some human pathogens harbor this class of enzymes. |
| first_indexed | 2024-03-10T20:38:14Z |
| format | Article |
| id | doaj.art-dddd1ae173074776af4488c80ae07c2e |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T20:38:14Z |
| publishDate | 2020-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-dddd1ae173074776af4488c80ae07c2e2023-11-19T20:55:10ZengMDPI AGBiomolecules2218-273X2020-04-0110456410.3390/biom10040564Tetrameric Structures of Inorganic CBS-Pyrophosphatases from Various Bacterial Species Revealed by Small-Angle X-ray Scattering in SolutionLiubov A. Dadinova0Ekaterina Yu. Soshinskaia1Cy M. Jeffries2Dmitri I. Svergun3Eleonora V. Shtykova4Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics” of Russian Academy of Sciences, Leninskiy prospect, 59, 119333 Moscow, RussiaShubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics” of Russian Academy of Sciences, Leninskiy prospect, 59, 119333 Moscow, RussiaEMBL, Hamburg Unit, c/o DESY, Notkestr. 85, Geb. 25a, 22607 Hamburg, GermanyEMBL, Hamburg Unit, c/o DESY, Notkestr. 85, Geb. 25a, 22607 Hamburg, GermanyShubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics” of Russian Academy of Sciences, Leninskiy prospect, 59, 119333 Moscow, RussiaQuaternary structure of CBS-pyrophosphatases (CBS-PPases), which belong to the PPases of family II, plays an important role in their function ensuring cooperative behavior of the enzymes. Despite an intensive research, high resolution structures of the full-length CBS-PPases are not yet available making it difficult to determine the signal transmission path from the regulatory to the active center. In the present work, small-angle X-ray scattering (SAXS) combined with size-exclusion chromatography was applied to determine the solution structures of the full-length wild-type CBS-PPases from three different bacterial species. Previously, in the absence of an experimentally determined full-length CBS-PPase structure, a homodimeric model of the enzyme based on known crystal structures of the CBS domain and family II PPase without this domain has been proposed. Our SAXS analyses demonstrate, for the first time, the existence of stable tetramers in solution for all studied CBS-PPases from different sources. Our findings show that further studies are required to establish the functional properties of these enzymes. This is important not only to enhance our understanding of the relation between CBS-PPases structure and function under normal conditions but also because some human pathogens harbor this class of enzymes.https://www.mdpi.com/2218-273X/10/4/564inorganic pyrophosphatasecystathionine-β-synthaseCBS-domainCBS-pyrophosphatasessize-exclusion chromatographymulti-angle laser light |
| spellingShingle | Liubov A. Dadinova Ekaterina Yu. Soshinskaia Cy M. Jeffries Dmitri I. Svergun Eleonora V. Shtykova Tetrameric Structures of Inorganic CBS-Pyrophosphatases from Various Bacterial Species Revealed by Small-Angle X-ray Scattering in Solution Biomolecules inorganic pyrophosphatase cystathionine-β-synthase CBS-domain CBS-pyrophosphatases size-exclusion chromatography multi-angle laser light |
| title | Tetrameric Structures of Inorganic CBS-Pyrophosphatases from Various Bacterial Species Revealed by Small-Angle X-ray Scattering in Solution |
| title_full | Tetrameric Structures of Inorganic CBS-Pyrophosphatases from Various Bacterial Species Revealed by Small-Angle X-ray Scattering in Solution |
| title_fullStr | Tetrameric Structures of Inorganic CBS-Pyrophosphatases from Various Bacterial Species Revealed by Small-Angle X-ray Scattering in Solution |
| title_full_unstemmed | Tetrameric Structures of Inorganic CBS-Pyrophosphatases from Various Bacterial Species Revealed by Small-Angle X-ray Scattering in Solution |
| title_short | Tetrameric Structures of Inorganic CBS-Pyrophosphatases from Various Bacterial Species Revealed by Small-Angle X-ray Scattering in Solution |
| title_sort | tetrameric structures of inorganic cbs pyrophosphatases from various bacterial species revealed by small angle x ray scattering in solution |
| topic | inorganic pyrophosphatase cystathionine-β-synthase CBS-domain CBS-pyrophosphatases size-exclusion chromatography multi-angle laser light |
| url | https://www.mdpi.com/2218-273X/10/4/564 |
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