Backbone and side chain 1H, 15N and 13C assignments for a thiol-disulphide oxidoreductase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125

• Published in: Biomolecular NMR Assignments
• Main Authors: Collins, Tony, Matzapetakis, Manolis, Santos, Helena
• Format: Article in Journal/Newspaper
• Language: English
• Published: Springer Verlag 2010
• Subjects: Cold-adapted enzymes; DsbA; Reduced oxidoreductase; Pseudoalteromonas haloplanktis TAC125; Ciências Naturais::Ciências Biológicas; Antarctic; The Antarctic; Bia; Antarc*
• Online Access: http://hdl.handle.net/1822/45779; https://doi.org/10.1007/s12104-010-9230-0

Enzymes produced by psychrophilic organisms have successfully overcome the low temperature challenge and evolved to maintain high catalytic rates in their permanently cold environments. As an initial step in our attempt to elucidate the cold-adaptation strategies used by these enzymes we report here the 1H, 15N and 13C assignments for the reduced form of a thiol-disulphide oxidoreductase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125. The NMR spectrometers are part of The National NMR Network (REDE/1517/RMN/2005), supported by ‘‘Programa Operacional Ciência e Inovação (POCTI) 2010’’ and Fundação para a Ciência e a Tecnologia (FCT). This work was funded by FCT, POCTI and FEDER; Projects POCI/BIA-PRO/57263/2004 and PTDC/BIO/70806/2006. TC is holder of a long term EMBO fellowship. MM is thankful to the Fundação para a Ciência e Tecnologia for its support through Programa Ciência 2007. ...