2XSU

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

Summary for 2XSU

• Entry DOI: 10.2210/pdb2xsu/pdb
• Related: 2XSR 2XSV
• Descriptor: CATECHOL 1,2 DIOXYGENASE, FE (III) ION, 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOINOSITOL, ... (4 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: ACINETOBACTER RADIORESISTENS
• Total number of polymer chains: 1
• Total formula weight: 35290.07

Authors

Micalella, C.,Martignon, S.,Bruno, S.,Rizzi, M. (deposition date: 2010-09-30, release date: 2010-10-13, Last modification date: 2023-12-20)

Primary citation

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

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

Experimental method

X-RAY DIFFRACTION (1.6 Å)