8QC6
Crystal Structure of NAD-dependent glycoside hydrolase from Arthrobacter sp. U41 in complex with NAD+ and sulfoquinovose (SQ)
Summary for 8QC6
| Entry DOI | 10.2210/pdb8qc6/pdb |
| Descriptor | Oxidoreductase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, sulfoquinovose, ... (4 entities in total) |
| Functional Keywords | nad(h)-dependent, glysoside hydrolase, sulfoquinovose, sulfoglycolysis, hydrolase |
| Biological source | Arthrobacter sp. U41 |
| Total number of polymer chains | 2 |
| Total formula weight | 87694.47 |
| Authors | Sharma, M.,Davies, G.J. (deposition date: 2023-08-25, release date: 2023-12-27, Last modification date: 2024-01-10) |
| Primary citation | Kaur, A.,Pickles, I.B.,Sharma, M.,Madeido Soler, N.,Scott, N.E.,Pidot, S.J.,Goddard-Borger, E.D.,Davies, G.J.,Williams, S.J. Widespread Family of NAD + -Dependent Sulfoquinovosidases at the Gateway to Sulfoquinovose Catabolism. J.Am.Chem.Soc., 145:28216-28223, 2023 Cited by PubMed Abstract: The sulfosugar sulfoquinovose (SQ) is produced by photosynthetic plants, algae, and cyanobacteria on a scale of 10 billion tons per annum. Its degradation, which is essential to allow cycling of its constituent carbon and sulfur, involves specialized glycosidases termed sulfoquinovosidases (SQases), which release SQ from sulfolipid glycoconjugates, so SQ can enter catabolism pathways. However, many SQ catabolic gene clusters lack a gene encoding a classical SQase. Here, we report the discovery of a new family of SQases that use an atypical oxidoreductive mechanism involving NAD as a catalytic cofactor. Three-dimensional X-ray structures of complexes with SQ and NAD provide insight into the catalytic mechanism, which involves transient oxidation at C3. Bioinformatic survey reveals this new family of NAD-dependent SQases occurs within sulfoglycolytic and sulfolytic gene clusters that lack classical SQases and is distributed widely including within clade bacteria, suggesting an important contribution to marine sulfur cycling. PubMed: 38100472DOI: 10.1021/jacs.3c11126 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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