8qc5 | pdb_00008qc5

crystal structure of NAD-dependent glycoside hydrolase from Arthrobacter sp. U41 in complex with NAD+ cofactor and citrate

spinqualitylabelsall models 8qc5, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8qc5 is a 2 chain structure with sequence from Arthrobacter sp. U41. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: CIT, NAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1C9WRL0_9MICC Publication Abstract from PubMed 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 Roseobacter clade bacteria, suggesting an important contribution to marine sulfur cycling. Widespread Family of NAD(+)-Dependent Sulfoquinovosidases at the Gateway to Sulfoquinovose Catabolism.,Kaur A, Pickles IB, Sharma M, Madeido Soler N, Scott NE, Pidot SJ, Goddard-Borger ED, Davies GJ, Williams SJ J Am Chem Soc. 2023 Dec 27;145(51):28216-28223. doi: 10.1021/jacs.3c11126. Epub , 2023 Dec 15. PMID:38100472 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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