Abstract
Enzymes of the aldehyde dehydrogenase (ALDH) superfamily catalyze the nicotinamide adenine dinucleotide-dependent oxidation of aldehydes to carboxylic acids. ALDHs are important in detoxification of aldehydes, amino acid metabolism, embryogenesis and development, neurotransmission, oxidative stress, and cancer. Mutations in genes encoding ALDHs cause metabolic disorders, including alcohol flush reaction (ALDH2), Sjögren–Larsson syndrome (ALDH3A2), hyperprolinemia type II (ALDH4A1), γ-hydroxybutyric aciduria (ALDH5A1), methylmalonic aciduria (ALDH6A1), pyridoxine dependent epilepsy (ALDH7A1), and hyperammonemia (ALDH18A1). We previously reported crystal structures and small-angle X-ray scattering (SAXS) analyses of ALDHs exhibiting dimeric, tetrameric, and hexameric oligomeric states (Luo et al., Biochemistry 54 (2015) 5513–5522; Luo et al., J. Mol. Biol. 425 (2013) 3106–3120). Herein I provide the SAXS curves, radii of gyration, and distance distribution functions for the three types of ALDH oligomer. The SAXS curves and associated analysis provide diagnostic fingerprints that allow rapid identification of the type of ALDH oligomer that is present in solution. The data sets provided here serve as a benchmark for characterizing oligomerization of ALDHs.
Highlights
Enzymes of the aldehyde dehydrogenase (ALDH) superfamily catalyze the nicotinamide adenine dinucleotide-dependent oxidation of aldehydes to carboxylic acids
ALDHs are important in detoxification of aldehydes, amino acid metabolism, embryogenesis and development, neurotransmission, oxidative stress, and cancer
We previously reported crystal structures and small-angle X-ray scattering (SAXS) analyses of ALDHs exhibiting dimeric, tetrameric, and hexameric oligomeric states (Luo et al, Biochemistry 54 (2015) 5513–5522; Luo et al, J
Summary
SAXS data files (.dat) and protein structure coordinate files (.pdb) Small-angle X-ray scattering (SAXS) data collected at Advanced Light Source Beamline 12.3.1 Buffer-subtracted, merged experimental scattering curves (.dat) Purified protein samples were subjected to size exclusion chromatography and shipped at 4 °C in 96-well trays to beamline 12.3.1. Data were collected by the beamline staff as part of the mail-in SAXS program at the SIBYLS beamline. The beamline staff provides the user with buffer-subtracted SAXS curves. SAXS curves and coordinates of crystal structures are provided as supplementary content. SAXS is a robust method for determining the oligomeric states of proteins in solution. SAXS provides a diagnostic fingerprint of ALDH oligomeric state and quaternary structure. The data sets provided here serve as a benchmark for characterizing ALDH oligomerization
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