2D51
Pentaketide chromone synthase (M207G mutant)
2D51 の概要
| エントリーDOI | 10.2210/pdb2d51/pdb |
| 関連するPDBエントリー | 1BQ6 1EE0 2D3M 2D52 |
| 分子名称 | pentaketide chromone synthase (2 entities in total) |
| 機能のキーワード | pentaketide chromone synthase, chalcone synthase, polyketide synthase, transferase |
| 由来する生物種 | Aloe arborescens |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 89583.06 |
| 構造登録者 | |
| 主引用文献 | Morita, H.,Kondo, S.,Oguro, S.,Noguchi, H.,Sugio, S.,Abe, I.,Kohno, T. Structural Insight into Chain-Length Control and Product Specificity of Pentaketide Chromone Synthase from Aloe arborescens Chem.Biol., 14:359-369, 2007 Cited by PubMed Abstract: The crystal structures of a wild-type and a mutant PCS, a novel plant type III polyketide synthase from a medicinal plant, Aloe arborescens, were solved at 1.6 A resolution. The crystal structures revealed that the pentaketide-producing wild-type and the octaketide-producing M207G mutant shared almost the same overall folding, and that the large-to-small substitution dramatically increases the volume of the polyketide-elongation tunnel by opening a gate to two hidden pockets behind the active site of the enzyme. The chemically inert active site residue 207 thus controls the number of condensations of malonyl-CoA, solely depending on the steric bulk of the side chain. These findings not only provided insight into the polyketide formation reaction, but they also suggested strategies for the engineered biosynthesis of polyketides. PubMed: 17462571DOI: 10.1016/j.chembiol.2007.02.003 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.6 Å) |
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