2xsu: Difference between revisions
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<StructureSection load='2xsu' size='340' side='right'caption='[[2xsu]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='2xsu' size='340' side='right'caption='[[2xsu]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xsu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2xsu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_radioresistens Acinetobacter radioresistens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XSU FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PIE:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOINOSITOL'>PIE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xsu OCA], [https://pdbe.org/2xsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xsu RCSB], [https://www.ebi.ac.uk/pdbsum/2xsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xsu ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xsu OCA], [https://pdbe.org/2xsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xsu RCSB], [https://www.ebi.ac.uk/pdbsum/2xsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xsu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9F103_ACIRA Q9F103_ACIRA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Acinetobacter radioresistens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bruno | [[Category: Bruno S]] | ||
[[Category: Martignon | [[Category: Martignon S]] | ||
[[Category: Micalella | [[Category: Micalella C]] | ||
[[Category: Rizzi | [[Category: Rizzi M]] | ||
Latest revision as of 13:38, 20 December 2023
Crystal structure of the A72G mutant of Acinetobacter radioresistens catechol 1,2 dioxygenaseCrystal structure of the A72G mutant of Acinetobacter radioresistens catechol 1,2 dioxygenase
Structural highlights
FunctionPublication Abstract from PubMedIntradiol-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. X-ray crystallography, mass spectrometry and single crystal microspectrophotometry: A multidisciplinary characterization of catechol 1,2 dioxygenase.,Micalella C, Martignon S, Bruno S, Pioselli B, Caglio R, Valetti F, Pessione E, Giunta C, Rizzi M Biochim Biophys Acta. 2010 Sep 22. PMID:20869471[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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