2R0P

K252c-soaked RebC

2R0P の概要

• エントリーDOI: 10.2210/pdb2r0p/pdb
• 関連するPDBエントリー: 2R0C 2R0G
• 分子名称: RebC, CHLORIDE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: flavin adenine dinucleotide, k252c, monooxygenase, oxidoreductase
• 由来する生物種: Lechevalieria aerocolonigenes
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 61059.97

構造登録者

Ryan, K.S.,Drennan, C.L. (登録日: 2007-08-20, 公開日: 2007-09-25, 最終更新日: 2023-08-30)

主引用文献

Ryan, K.S.,Howard-Jones, A.R.,Hamill, M.J.,Elliott, S.J.,Walsh, C.T.,Drennan, C.L.
Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC
Proc.Natl.Acad.Sci.Usa, 104:15311-15316, 2007

PubMed Abstract: The biosynthesis of rebeccamycin, an antitumor compound, involves the remarkable eight-electron oxidation of chlorinated chromopyrrolic acid. Although one rebeccamycin biosynthetic enzyme is capable of generating low levels of the eight-electron oxidation product on its own, a second protein, RebC, is required to accelerate product formation and eliminate side reactions. However, the mode of action of RebC was largely unknown. Using crystallography, we have determined a likely function for RebC as a flavin hydroxylase, captured two snapshots of its dynamic catalytic cycle, and trapped a reactive molecule, a putative substrate, in its binding pocket. These studies strongly suggest that the role of RebC is to sequester a reactive intermediate produced by its partner protein and to react with it enzymatically, preventing its conversion to a suite of degradation products that includes, at low levels, the desired product.

PubMed: 17873060
DOI: 10.1073/pnas.0707190104

実験手法

X-RAY DIFFRACTION (2.1 Å)