7w5l

The crystal structure of the oxidized form of Gluconobacter oxydans WSH-004 SNDH

spinqualitylabelsall models 7w5l, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7w5l is a 1 chain structure with sequence from Gluconobacter oxydans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q47943_GLUOY Publication Abstract from PubMed L-Sorbosone dehydrogenase (SNDH) is a key enzyme involved in the biosynthesis of 2-keto-L-gulonic acid , which is a direct precursor for the industrial scale production of vitamin C. Elucidating the structure and the catalytic mechanism is essential for improving SNDH performance. By solving the crystal structures of SNDH from Gluconobacter oxydans WSH-004, a reversible disulfide bond between Cys295 and the catalytic Cys296 residues is discovered. It allowed SNDH to switch between oxidation and reduction states, resulting in opening or closing the substrate pocket. Moreover, the Cys296 is found to affect the NADP(+) binding pose with SNDH. Combining the in vitro biochemical and site-directed mutagenesis studies, the redox-based dynamic regulation and the catalytic mechanisms of SNDH are proposed. Moreover, the mutants with enhanced activity are obtained by extending substrate channels. This study not only elucidates the physiological control mechanism of the dehydrogenase, but also provides a theoretical basis for engineering similar enzymes. Structural Insight into the Catalytic Mechanisms of an L-Sorbosone Dehydrogenase.,Li D, Deng Z, Hou X, Qin Z, Wang X, Yin D, Chen Y, Rao Y, Chen J, Zhou J Adv Sci (Weinh). 2023 Oct;10(30):e2301955. doi: 10.1002/advs.202301955. Epub 2023 , Sep 7. PMID:37679059 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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