4M25
Crystal structure of non-heme iron oxygenase OrfP in complex with Fe and alpha-ketoglutaric acid
4M25 の概要
エントリーDOI | 10.2210/pdb4m25/pdb |
関連するPDBエントリー | 4M23 4M26 4M27 4M2C 4M2E 4M2F 4M2G 4M2I 4M2J 4M2K 4M2M |
分子名称 | L-arginine beta-hydroxylase, FE (III) ION, 2-OXOGLUTARIC ACID, ... (4 entities in total) |
機能のキーワード | hydroxylase, fe binding, oxidoreductase |
由来する生物種 | Streptomyces lavendulae |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 165783.48 |
構造登録者 | Chang, C.Y.,Liu, Y.C.,Lyu, S.Y.,Wu, C.C.,Li, T.L. (登録日: 2013-08-05, 公開日: 2014-06-25, 最終更新日: 2023-11-08) |
主引用文献 | Chang, C.Y.,Lyu, S.Y.,Liu, Y.C.,Hsu, N.S.,Wu, C.C.,Tang, C.F.,Lin, K.H.,Ho, J.Y.,Wu, C.J.,Tsai, M.D.,Li, T.L. Biosynthesis of streptolidine involved two unexpected intermediates produced by a dihydroxylase and a cyclase through unusual mechanisms. Angew.Chem.Int.Ed.Engl., 53:1943-1948, 2014 Cited by PubMed Abstract: Streptothricin-F (STT-F), one of the early-discovered antibiotics, consists of three components, a β-lysine homopolymer, an aminosugar D-gulosamine, and an unusual bicyclic streptolidine. The biosynthesis of streptolidine is a long-lasting but unresolved puzzle. Herein, a combination of genetic/biochemical/structural approaches was used to unravel this problem. The STT gene cluster was first sequenced from a Streptomyces variant BCRC 12163, wherein two gene products OrfP and OrfR were characterized in vitro to be a dihydroxylase and a cyclase, respectively. Thirteen high-resolution crystal structures for both enzymes in different reaction intermediate states were snapshotted to help elucidate their catalytic mechanisms. OrfP catalyzes an Fe(II) -dependent double hydroxylation reaction converting L-Arg into (3R,4R)-(OH)2 -L-Arg via (3S)-OH-L-Arg, while OrfR catalyzes an unusual PLP-dependent elimination/addition reaction cyclizing (3R,4R)-(OH)2 -L-Arg to the six-membered (4R)-OH-capreomycidine. The biosynthetic mystery finally comes to light as the latter product was incorporation into STT-F by a feeding experiment. PubMed: 24505011DOI: 10.1002/anie.201307989 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.84 Å) |
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