4eip | pdb_00004eip

Native and K252c bound RebC-10x

spinqualitylabelsall models 4eip, resolution 2.33Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4eip is a 2 chain structure with sequence from Lechevalieria aerocolonigenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD, K2C Related: 2r0c, 2r0p, 4eiq Gene: rbmD, rebC (Lechevalieria aerocolonigenes) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed The indolocarbazole biosynthetic enzymes StaC, InkE, RebC, and AtmC mediate the degree of oxidation of chromopyrrolic acid on route to the natural products staurosporine, K252a, rebeccamycin, and AT2433-A1, respectively. Here, we show that StaC and InkE, which mediate a net 4-electron oxidation, bind FAD with a micromolar K(d), whereas RebC and AtmC, which mediate a net 8-electron oxidation, bind FAD with a nanomolar K(d) while displaying the same FAD redox properties. We further create RebC-10x, a RebC protein with ten StaC-like amino acid substitutions outside of previously characterized FAD-binding motifs and the complementary StaC-10x. We find that these mutations mediate both FAD affinity and product specificity, with RebC-10x displaying higher StaC activity than StaC itself. X-ray structures of this StaC catalyst identify the substrate of StaC as 7-carboxy-K252c and suggest a unique mechanism for this FAD-dependent enzyme. An Unusual Role for a Mobile Flavin in StaC-like Indolocarbazole Biosynthetic Enzymes.,Goldman PJ, Ryan KS, Hamill MJ, Howard-Jones AR, Walsh CT, Elliott SJ, Drennan CL Chem Biol. 2012 Jul 27;19(7):855-65. PMID:22840773 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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