Biochemical and structural studies of two tetrameric nucleoside 2′-deoxyribosyltransferases from psychrophilic and mesophilic bacteria: Insights into cold-adaptation

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Fernández Lucas, Jesús and Acebrón Ávalos, Iván and Wu, Ruiying Y. and Alfaro, Yohana and Acosta, Javier and Kaminski, Pierre A. and Arroyo Sánchez, Miguel and Joachimiak, Andrzej and Nocek, Boguslaw P. and Mata Riesco, Isabel de la and Mancheño Gómez, José Miguel (2021) Biochemical and structural studies of two tetrameric nucleoside 2′-deoxyribosyltransferases from psychrophilic and mesophilic bacteria: Insights into cold-adaptation. International Journal of Biological Macromolecules, 192 . pp. 138-150. ISSN 0141-8130, ESSN: 1879-0003

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Official URL: https://doi.org/10.1016/j.ijbiomac.2021.09.164



Abstract

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.


Item Type:Article
Uncontrolled Keywords:2′-Deoxyribosyltransferases; Crystal structure; Psychrophilic enzymes
Subjects:Medical sciences > Biology > Biochemistry
ID Code:73530
Deposited On:08 Jul 2022 15:16
Last Modified:01 Aug 2022 12:00

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