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3G7D

Native PhpD with Cadmium Atoms

3G7D の概要
エントリーDOI10.2210/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
Nair, S.K. (登録日: 2009-02-09, 公開日: 2009-06-09, 最終更新日: 2024-11-27)
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: 19516340
DOI: 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
Validation report summary of 3g7d
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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