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Publication Abstract from PubMed

The primary role of yeast Ara1, previously mis-annotated as a D-arabinose dehydrogenase, is to catalyze the reduction of a variety of toxic alpha,beta-dicarbonyl compounds using NADPH as a cofactor at physiological pH levels. Here, crystal structures of Ara1 in apo and NADPH-complexed forms are presented at 2.10 and 2.00 A resolution, respectively. Ara1 exists as a homodimer, each subunit of which adopts an (alpha/beta)8-barrel structure and has a highly conserved cofactor-binding pocket. Structural comparison revealed that induced fit upon NADPH binding yielded an intact active-site pocket that recognizes the substrate. Moreover, the crystal structures combined with computational simulation defined an open substrate-binding site to accommodate various substrates that possess a dicarbonyl group.

Structures of Saccharomyces cerevisiaeD-arabinose dehydrogenase Ara1 and its complex with NADPH: implications for cofactor-assisted substrate recognition.,Hu XQ, Guo PC, Ma JD, Li WF Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1190-5. doi:, 10.1107/S1744309113026857. Epub 2013 Oct 26. PMID:24192347^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.