4ha9

Structural insights into the reduction mechanism of Saccharomyces cerevisia Riboflavin Biosynthesis Reductase Rib7

spinqualitylabelsall models 4ha9, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ha9 is a 2 chain structure with sequence from Saccharomyces cerevisiae s288c. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NDP Related: 4ha7 Gene: RIB7, YBR153W, YBR1203 (Saccharomyces cerevisiae S288c) Activity: 2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5'-phosphate reductase, with EC number 1.1.1.302 Resources: FirstGlance, OCA, RCSB, PDBsum Function [RIB7_YEAST] Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate (Probable). Publication Abstract from PubMed Saccharomyces cerevisiae RIB7 (ScRIB7) is a potent target for anti-fungal agents because of its involvement in the riboflavin biosynthesis pathway as a NADPH-dependent reductase. However, the catalytic mechanism of riboflavin biosynthesis reductase (RBSRs) is controversial, and enzyme structure information is still lacking in eukaryotes. Here we report the crystal structure of Saccharomyces cerevisiae RIB7 at 2.10 A resolution and its complex with NADPH at 2.35 A resolution. ScRIB7 exists as a stable homodimer, and each subunit consists of nine central beta-sheets flanked by five helices, resembling the structure of RIB7 homologues. A conserved G(76)-X-G(78)-Xn-G(181)-G(182) motif is present at the NADPH pyrophosphate group binding site. Activity assays confirmed the necessity of Thr79, Asp83, Glu180 and Gly182 for the activity of ScRIB7. Substrate preference of ScRIB7 was altered by mutating one residue (Thr35) to a Lysine, implying that ScRIB7 Thr35 and its corresponding residue, a lysine in bacteria, are important in substrate-specific recognition. Structural and functional insights into Saccharomyces cerevisiae riboflavin biosynthesis reductase RIB7.,Lv Z, Sun J, Liu Y PLoS One. 2013 Apr 19;8(4):e61249. doi: 10.1371/journal.pone.0061249. Print 2013. PMID:23620735 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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