RT Journal Article
T1 Biochemical and structural studies of two tetrameric nucleoside 2′-deoxyribosyltransferases from psychrophilic and mesophilic bacteria: Insights into cold-adaptation
A1 Fernández Lucas, Jesús
A1 Acebrón Ávalos, Iván
A1 Wu, Ruiying Y.
A1 Alfaro, Yohana
A1 Acosta, Javier
A1 Kaminski, Pierre A.
A1 Arroyo Sánchez, Miguel
A1 Joachimiak, Andrzej
A1 Nocek, Boguslaw P.
A1 De La Mata Riesco, Mª Isabel
A1 Mancheño Gómez, José Miguel
AB 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.
PB Elsevier
SN 0141-8130, ESSN: 1879-0003
YR 2021
FD 2021-10-05
LK https://hdl.handle.net/20.500.14352/4972
UL https://hdl.handle.net/20.500.14352/4972
LA eng
NO Ministerio de Ciencia e Innovación (MICINN)
NO Comunidad de Madrid
NO Fundación Santander
NO Instituto Nacional de la Salud (INS)
NO U.S. Department of Energy (DOE)
NO Argonne National Laboratory
DS Docta Complutense
RD 10 abr 2025