4IJC
Crystal structure of arabinose dehydrogenase Ara1 from Saccharomyces cerevisiae
Summary for 4IJC
| Entry DOI | 10.2210/pdb4ijc/pdb |
| Related | 4IJR |
| Descriptor | D-arabinose dehydrogenase [NAD(P)+] heavy chain, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | beta barrel, tim barrel, oxidoreductase |
| Biological source | Saccharomyces cerevisiae (yeast) |
| Cellular location | Cytoplasm: P38115 |
| Total number of polymer chains | 2 |
| Total formula weight | 78341.24 |
| Authors | Hu, X.Q.,Guo, P.C.,Li, W.F.,Zhou, C.Z. (deposition date: 2012-12-21, release date: 2013-11-27, Last modification date: 2023-11-08) |
| Primary citation | Hu, X.Q.,Guo, P.C.,Ma, J.D.,Li, W.F. Structures of Saccharomyces cerevisiaeD-arabinose dehydrogenase Ara1 and its complex with NADPH: implications for cofactor-assisted substrate recognition Acta Crystallogr.,Sect.F, 69:1190-1195, 2013 Cited by PubMed Abstract: The primary role of yeast Ara1, previously mis-annotated as a D-arabinose dehydrogenase, is to catalyze the reduction of a variety of toxic α,β-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 Å resolution, respectively. Ara1 exists as a homodimer, each subunit of which adopts an (α/β)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. PubMed: 24192347DOI: 10.1107/S1744309113026857 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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