2XSU
Crystal structure of the A72G mutant of Acinetobacter radioresistens catechol 1,2 dioxygenase
2XSU の概要
| エントリーDOI | 10.2210/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: 20869471DOI: 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) |
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