Biochemical and structural studies of two tetrameric nucleoside 2′-deoxyribosyltransferases from psychrophilic and mesophilic bacteria: insights into cold-adaptation
Nucleoside 2′-deoxyribosyltransferases (NDTs) catalyze the cleavage of glycosidic bonds of 2′-deoxynucleosides and the following transfer of the 2′-deoxyribose moiety to acceptor nucleobases. Here, we report the crystal structures and biochemical properties of the first tetrameric NDTs: the type I N...
- Autores:
-
Fernández-Lucas, Jesús
Acebrón, Iván
Wu, Ruiying Y.
Alfaro, Yohana
Acosta, Javier
Kaminski, Pierre Alexandre
Arroyo, Miguel
Joachimiak, Andrzej
Nocek, Boguslaw
de la Mata, Isabel
Mancheño, José M.
- Tipo de recurso:
- Article of journal
- Fecha de publicación:
- 2020
- Institución:
- Corporación Universidad de la Costa
- Repositorio:
- REDICUC - Repositorio CUC
- Idioma:
- eng
- OAI Identifier:
- oai:repositorio.cuc.edu.co:11323/9064
- Acceso en línea:
- https://hdl.handle.net/11323/9064
https://doi.org/10.1016/j.ijbiomac.2021.09.164
https://repositorio.cuc.edu.co/
- Palabra clave:
- 2′-Deoxyribosyltransferases
Crystal structure
Psychrophilic enzymes
- Rights
- embargoedAccess
- License
- Copyright © 2022 Elsevier B.V.
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| dc.title.eng.fl_str_mv |
Biochemical and structural studies of two tetrameric nucleoside 2′-deoxyribosyltransferases from psychrophilic and mesophilic bacteria: insights into cold-adaptation |
| title |
Biochemical and structural studies of two tetrameric nucleoside 2′-deoxyribosyltransferases from psychrophilic and mesophilic bacteria: insights into cold-adaptation |
| spellingShingle |
Biochemical and structural studies of two tetrameric nucleoside 2′-deoxyribosyltransferases from psychrophilic and mesophilic bacteria: insights into cold-adaptation 2′-Deoxyribosyltransferases Crystal structure Psychrophilic enzymes |
| title_short |
Biochemical and structural studies of two tetrameric nucleoside 2′-deoxyribosyltransferases from psychrophilic and mesophilic bacteria: insights into cold-adaptation |
| title_full |
Biochemical and structural studies of two tetrameric nucleoside 2′-deoxyribosyltransferases from psychrophilic and mesophilic bacteria: insights into cold-adaptation |
| title_fullStr |
Biochemical and structural studies of two tetrameric nucleoside 2′-deoxyribosyltransferases from psychrophilic and mesophilic bacteria: insights into cold-adaptation |
| title_full_unstemmed |
Biochemical and structural studies of two tetrameric nucleoside 2′-deoxyribosyltransferases from psychrophilic and mesophilic bacteria: insights into cold-adaptation |
| title_sort |
Biochemical and structural studies of two tetrameric nucleoside 2′-deoxyribosyltransferases from psychrophilic and mesophilic bacteria: insights into cold-adaptation |
| dc.creator.fl_str_mv |
Fernández-Lucas, Jesús Acebrón, Iván Wu, Ruiying Y. Alfaro, Yohana Acosta, Javier Kaminski, Pierre Alexandre Arroyo, Miguel Joachimiak, Andrzej Nocek, Boguslaw de la Mata, Isabel Mancheño, José M. |
| dc.contributor.author.spa.fl_str_mv |
Fernández-Lucas, Jesús Acebrón, Iván Wu, Ruiying Y. Alfaro, Yohana Acosta, Javier Kaminski, Pierre Alexandre Arroyo, Miguel Joachimiak, Andrzej Nocek, Boguslaw de la Mata, Isabel Mancheño, José M. |
| dc.subject.proposal.eng.fl_str_mv |
2′-Deoxyribosyltransferases Crystal structure Psychrophilic enzymes |
| topic |
2′-Deoxyribosyltransferases Crystal structure Psychrophilic enzymes |
| description |
Nucleoside 2′-deoxyribosyltransferases (NDTs) catalyze the cleavage of glycosidic bonds of 2′-deoxynucleosides and the following transfer of the 2′-deoxyribose moiety to acceptor nucleobases. Here, we report the crystal structures and biochemical properties of the first tetrameric NDTs: the type I NDT from the mesophilic bacterium Enterococcus faecalis V583 (EfPDT) and the type II NDT from the bacterium Desulfotalea psychrophila (DpNDT), the first psychrophilic NDT. This novel structural and biochemical data permitted an exhaustive comparative analysis aimed to shed light into the basis of the high global stability of the psychrophilic DpNDT, which has a higher melting temperature than EfPDT (58.5 °C versus 54.4 °C) or other mesophilic NDTs. DpNDT possesses a combination of unusual structural motifs not present neither in EfPDT nor any other NDT that most probably contribute to its global stability, in particular, a large aliphatic isoleucine-leucine-valine (ILV) bundle accompanied by a vicinal disulfide bridge and also an intersubunit disulfide bridge, the first described for an NDT. The functional and structural features of DpNDT do not fit the standard features of psychrophilic enzymes, which lead us to consider the implication of (sub)cellular levels together with the protein level in the adaptation of enzymatic activity to low temperatures. |
| publishDate |
2020 |
| dc.date.issued.none.fl_str_mv |
2020-12-01 |
| dc.date.accessioned.none.fl_str_mv |
2022-03-10T19:04:46Z |
| dc.date.available.none.fl_str_mv |
2022-12-01 2022-03-10T19:04:46Z |
| dc.type.spa.fl_str_mv |
Artículo de revista |
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http://purl.org/coar/resource_type/c_2df8fbb1 |
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http://purl.org/coar/resource_type/c_6501 |
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Text |
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info:eu-repo/semantics/article |
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http://purl.org/redcol/resource_type/ART |
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info:eu-repo/semantics/acceptedVersion |
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acceptedVersion |
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0141-8130 |
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https://hdl.handle.net/11323/9064 |
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https://doi.org/10.1016/j.ijbiomac.2021.09.164 |
| dc.identifier.doi.spa.fl_str_mv |
10.1016/j.ijbiomac.2021.09.164 |
| dc.identifier.eissn.spa.fl_str_mv |
1879-0003 |
| dc.identifier.instname.spa.fl_str_mv |
Corporación Universidad de la Costa |
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REDICUC - Repositorio CUC |
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https://repositorio.cuc.edu.co/ |
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0141-8130 10.1016/j.ijbiomac.2021.09.164 1879-0003 Corporación Universidad de la Costa REDICUC - Repositorio CUC |
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https://hdl.handle.net/11323/9064 https://doi.org/10.1016/j.ijbiomac.2021.09.164 https://repositorio.cuc.edu.co/ |
| dc.language.iso.none.fl_str_mv |
eng |
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eng |
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International Journal of Biological Macromolecules |
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Fernández-Lucas, JesúsAcebrón, IvánWu, Ruiying Y.Alfaro, YohanaAcosta, JavierKaminski, Pierre AlexandreArroyo, MiguelJoachimiak, AndrzejNocek, Boguslawde la Mata, IsabelMancheño, José M.2022-03-10T19:04:46Z2022-12-012022-03-10T19:04:46Z2020-12-010141-8130https://hdl.handle.net/11323/9064https://doi.org/10.1016/j.ijbiomac.2021.09.16410.1016/j.ijbiomac.2021.09.1641879-0003Corporación Universidad de la CostaREDICUC - Repositorio CUChttps://repositorio.cuc.edu.co/Nucleoside 2′-deoxyribosyltransferases (NDTs) catalyze the cleavage of glycosidic bonds of 2′-deoxynucleosides and the following transfer of the 2′-deoxyribose moiety to acceptor nucleobases. Here, we report the crystal structures and biochemical properties of the first tetrameric NDTs: the type I NDT from the mesophilic bacterium Enterococcus faecalis V583 (EfPDT) and the type II NDT from the bacterium Desulfotalea psychrophila (DpNDT), the first psychrophilic NDT. This novel structural and biochemical data permitted an exhaustive comparative analysis aimed to shed light into the basis of the high global stability of the psychrophilic DpNDT, which has a higher melting temperature than EfPDT (58.5 °C versus 54.4 °C) or other mesophilic NDTs. DpNDT possesses a combination of unusual structural motifs not present neither in EfPDT nor any other NDT that most probably contribute to its global stability, in particular, a large aliphatic isoleucine-leucine-valine (ILV) bundle accompanied by a vicinal disulfide bridge and also an intersubunit disulfide bridge, the first described for an NDT. The functional and structural features of DpNDT do not fit the standard features of psychrophilic enzymes, which lead us to consider the implication of (sub)cellular levels together with the protein level in the adaptation of enzymatic activity to low temperatures.13 páginasapplication/pdfengElsevierNetherlandsCopyright © 2022 Elsevier B.V.Atribución-NoComercial-SinDerivadas 4.0 Internacional (CC BY-NC-ND 4.0)https://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/embargoedAccesshttp://purl.org/coar/access_right/c_f1cfBiochemical and structural studies of two tetrameric nucleoside 2′-deoxyribosyltransferases from psychrophilic and mesophilic bacteria: insights into cold-adaptationArtículo de revistahttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1Textinfo:eu-repo/semantics/articlehttp://purl.org/redcol/resource_type/ARTinfo:eu-repo/semantics/acceptedVersionhttps://www.sciencedirect.com/science/article/pii/S0141813021020924?via%3DihubInternational Journal of Biological Macromolecules[1] S.A. 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Genet., 10 (2009), pp. 715-724, 10.1038/nrg26621501381922′-DeoxyribosyltransferasesCrystal structurePsychrophilic enzymesPublicationORIGINALBiochemical and structural studies.pdfBiochemical and structural studies.pdfapplication/pdf10184809https://repositorio.cuc.edu.co/bitstreams/c7fb20df-fd3b-46ca-b708-a44777934f7c/download0e51e3b987528c4bcd85acc404d634a1MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-83196https://repositorio.cuc.edu.co/bitstreams/db1d5335-0701-48d9-8b64-117c453c3fc9/downloade30e9215131d99561d40d6b0abbe9badMD52TEXTBiochemical and structural studies.pdf.txtBiochemical and structural studies.pdf.txttext/plain84461https://repositorio.cuc.edu.co/bitstreams/6210715e-1cb1-48c3-99e9-e47f3ecc447a/downloadad89a90ac9f8a92711aae79f6c0718bcMD53THUMBNAILBiochemical and structural studies.pdf.jpgBiochemical and structural 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