3G7D
Native PhpD with Cadmium Atoms
3G7D の概要
| エントリーDOI | 10.2210/pdb3g7d/pdb |
| 分子名称 | PhpD, CADMIUM ION (3 entities in total) |
| 機能のキーワード | non heme fe(ii) dioxygenase, cupin, biosynthetic protein |
| 由来する生物種 | Streptomyces viridochromogenes |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 49844.15 |
| 構造登録者 | |
| 主引用文献 | Cicchillo, R.M.,Zhang, H.,Blodgett, J.A.,Whitteck, J.T.,Li, G.,Nair, S.K.,van der Donk, W.A.,Metcalf, W.W. An unusual carbon-carbon bond cleavage reaction during phosphinothricin biosynthesis. Nature, 459:871-874, 2009 Cited by PubMed Abstract: Natural products containing phosphorus-carbon bonds have found widespread use in medicine and agriculture. One such compound, phosphinothricin tripeptide, contains the unusual amino acid phosphinothricin attached to two alanine residues. Synthetic phosphinothricin (glufosinate) is a component of two top-selling herbicides (Basta and Liberty), and is widely used with resistant transgenic crops including corn, cotton and canola. Recent genetic and biochemical studies showed that during phosphinothricin tripeptide biosynthesis 2-hydroxyethylphosphonate (HEP) is converted to hydroxymethylphosphonate (HMP). Here we report the in vitro reconstitution of this unprecedented C(sp(3))-C(sp(3)) bond cleavage reaction and X-ray crystal structures of the enzyme. The protein is a mononuclear non-haem iron(ii)-dependent dioxygenase that converts HEP to HMP and formate. In contrast to most other members of this family, the oxidative consumption of HEP does not require additional cofactors or the input of exogenous electrons. The current study expands the scope of reactions catalysed by the 2-His-1-carboxylate mononuclear non-haem iron family of enzymes. PubMed: 19516340DOI: 10.1038/nature07972 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






