6fjh

Crystal structure of the seleniated LkcE from Streptomyces rochei

spinqualitylabelsall models 6fjh, resolution 3.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fjh is a 2 chain structure with sequence from Streptomyces rochei subsp. volubilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.15Å Ligands: FAD, MSE, NA, OXY Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G4V2H3_STRRO Publication Abstract from PubMed Acquisition of new catalytic activity is a relatively rare evolutionary event. A striking example appears in the pathway to the antibiotic lankacidin, as a monoamine oxidase (MAO) family member, LkcE, catalyzes both an unusual amide oxidation, and a subsequent intramolecular Mannich reaction to form the polyketide macrocycle. We report evidence here for the molecular basis for this dual activity. The reaction sequence involves several essential active site residues and a conformational change likely comprising an interdomain hinge movement. These features, which have not previously been described in the MAO family, both depend on a unique dimerization mode relative to all structurally characterized members. Taken together, these data add weight to the idea that designing new multifunctional enzymes may require changes in both architecture and catalytic machinery. Encouragingly, however, our data also show LkcE to bind alternative substrates, supporting its potential utility as a general cyclization catalyst in synthetic biology. Insights into a dual function amide oxidase/macrocyclase from lankacidin biosynthesis.,Dorival J, Risser F, Jacob C, Collin S, Drager G, Paris C, Chagot B, Kirschning A, Gruez A, Weissman KJ Nat Commun. 2018 Sep 28;9(1):3998. doi: 10.1038/s41467-018-06323-w. PMID:30266997 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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