3x27

Structure of McbB in complex with tryptophan

spinqualitylabelsall models 3x27, resolution 2.48Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3x27 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: TRP NonStd Res: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The beta-carboline (betaC) alkaloids occur throughout nature and exhibit diverse biological activities. In contrast to betaC alkaloid synthesis in plants, the biosynthesis in microorganisms remains poorly understood. The recently reported McbB from Marinactinospora thermotolerans is a novel enzyme proposed to catalyze the Pictet-Spengler (PS) reaction of L-tryptophan and oxaloacetaldehyde to produce the betaC scaffold of marinacarbolines. In this study, we solved the crystal structure of McbB complexed with L-tryptophan at 2.48 A resolution, which revealed the novel protein folding of McbB and the totally different structure from those of other PS condensation catalyzing enzymes, such as strictosidine synthase and norcoclaurine synthase from plants. Structural analysis and site-directed mutagenesis confirmed that the previously proposed catalytic Glu97 at the active-site center functions as an acid and base catalyst. Remarkably, the structure-based mutants R72A and H87A, with expanded active-site cavities, newly accepted bulky phenylglyoxal as the aldehyde substrate, to produce 1-benzoyl-3-carboxy-beta-carboline. Structural Basis for beta-Carboline Alkaloid Production by the Microbial Homodimeric Enzyme McbB.,Mori T, Hoshino S, Sahashi S, Wakimoto T, Matsui T, Morita H, Abe I Chem Biol. 2015 Jul 23;22(7):898-906. doi: 10.1016/j.chembiol.2015.06.006. Epub, 2015 Jun 25. PMID:26120001 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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