4HA9

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

4HA9 の概要

• エントリーDOI: 10.2210/pdb4ha9/pdb
• 関連するPDBエントリー: 4HA7
• 分子名称: 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: reductase, nadph binding, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55860.62

構造登録者

Lv, Z.,Sun, J.,Liu, Y. (登録日: 2012-09-25, 公開日: 2013-09-04, 最終更新日: 2024-02-28)

主引用文献

Lv, Z.,Sun, J.,Liu, Y.
Structural and functional insights into Saccharomyces cerevisiae riboflavin biosynthesis reductase RIB7.
Plos One, 8:e61249-e61249, 2013

PubMed Abstract: 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 Å resolution and its complex with NADPH at 2.35 Å resolution. ScRIB7 exists as a stable homodimer, and each subunit consists of nine central β-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.

PubMed: 23620735
DOI: 10.1371/journal.pone.0061249

実験手法

X-RAY DIFFRACTION (2.35 Å)