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2XSU

Crystal structure of the A72G mutant of Acinetobacter radioresistens catechol 1,2 dioxygenase

2XSU の概要
エントリーDOI10.2210/pdb2xsu/pdb
関連するPDBエントリー2XSR 2XSV
分子名称CATECHOL 1,2 DIOXYGENASE, FE (III) ION, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoinositol, ... (4 entities in total)
機能のキーワードoxidoreductase
由来する生物種ACINETOBACTER RADIORESISTENS
タンパク質・核酸の鎖数1
化学式量合計35290.07
構造登録者
Micalella, C.,Martignon, S.,Bruno, S.,Rizzi, M. (登録日: 2010-09-30, 公開日: 2010-10-13, 最終更新日: 2025-12-24)
主引用文献Micalella, C.,Martignon, S.,Bruno, S.,Pioselli, B.,Caglio, R.,Valetti, F.,Pessione, E.,Giunta, C.,Rizzi, M.
X-Ray Crystallography, Mass Spectrometry and Single Crystal Microspectrophotometry: A Multidisciplinary Characterization of Catechol 1,2 Dioxygenase.
Biochim.Biophys.Acta, 1814:817-, 2011
Cited by
PubMed Abstract: Intradiol-cleaving catechol 1,2 dioxygenases are Fe(III) dependent enzymes that act on catechol and substituted catechols, including chlorocatechols pollutants, by inserting molecular oxygen in the aromatic ring. Members of this class are the object of intense biochemical investigations aimed at the understanding of their catalytic mechanism, particularly for designing mutants with selected catalytic properties. We report here an in depth investigation of catechol 1,2 dioxygenase IsoB from Acinetobacter radioresistens LMG S13 and its A72G and L69A mutants. By applying a multidisciplinary approach that includes high resolution X-rays crystallography, mass spectrometry and single crystal microspectrophotometry, we characterised the phospholipid bound to the enzyme and provided a structural framework to understand the inversion of substrate specificity showed by the mutants. Our results might be of help for the rational design of enzyme mutants showing a biotechnologically relevant substrate specificity, particularly to be used in bioremediation. This article is part of a Special Issue entitled: Protein Structure and Function in the Crystalline State.
PubMed: 20869471
DOI: 10.1016/J.BBAPAP.2010.09.008
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.6 Å)
構造検証レポート
Validation report summary of 2xsu
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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