6a3g

Levoglucosan dehydrogenase, complex with NADH

spinqualitylabelsall models 6a3g, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6a3g is a 4 chain structure with sequence from Pseudarthrobacter phenanthrenivorans Sphe3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: NAI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F0M433_PSEPM Publication Abstract from PubMed Levoglucosan is the 1,6-anhydrosugar of D-glucose formed by pyrolysis of glucans and is found in the environment and industrial waste. Two types of microbial levoglucosan metabolic pathways are known. Although the eukaryotic pathway involving levoglucosan kinase has been well studied, the bacterial pathway involving levoglucosan dehydrogenase (LGDH) has not been well investigated. Here, we identified and cloned the lgdh gene from the bacterium Pseudarthrobacter phenanthrenivorans and characterized the recombinant protein. The enzyme exhibited high substrate specificity toward levoglucosan and NAD(+) for the oxidative reaction and was confirmed to be LGDH. LGDH also showed weak activities (~4%) toward L-sorbose and 1,5-anhydro-D-glucitol. The reverse (reductive) reaction using 3-keto levoglucosan and NADH exhibited significantly lower Km and higher kcat values than those of the forward reaction. The crystal structures of LGDH in the apo and complex forms with NADH, NADH + levoglucosan, and NADH + L-sorbose revealed that LGDH has a typical fold of Gfo/Idh/MocA family proteins, similar to those of scyllo-inositol dehydrogenase, aldose-aldose oxidoreductase, 1,5-anhydro-D-fructose reductase, and glucose-fructose oxidoreductase. The crystal structures also disclosed that the active site of LGDH is distinct from those of these enzymes. The LGDH active site extensively recognized the levoglucosan molecule with six hydrogen bonds, and the C3 atom of levoglucosan was closely located to the C4 atom of NADH nicotinamide. Our study is the first molecular characterization of LGDH, providing evidence for C3-specific oxidation, and representing a starting point for future biotechnological use of LGDH and levoglucosan-metabolizing bacteria. Identification, functional characterization, and crystal structure determination of bacterial levoglucosan dehydrogenase.,Sugiura M, Nakahara M, Yamada C, Arakawa T, Kitaoka M, Fushinobu S J Biol Chem. 2018 Sep 17. pii: RA118.004963. doi: 10.1074/jbc.RA118.004963. PMID:30224354 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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