3ej3: Difference between revisions
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<StructureSection load='3ej3' size='340' side='right'caption='[[3ej3]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='3ej3' size='340' side='right'caption='[[3ej3]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ej3]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3ej3]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_pavonaceae Pseudomonas pavonaceae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EJ3 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]] 1.7Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=3ej3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ej3 OCA], [https://pdbe.org/3ej3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ej3 RCSB], [https://www.ebi.ac.uk/pdbsum/3ej3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ej3 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=3ej3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ej3 OCA], [https://pdbe.org/3ej3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ej3 RCSB], [https://www.ebi.ac.uk/pdbsum/3ej3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ej3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9EV85_PSEPV Q9EV85_PSEPV] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pseudomonas pavonaceae]] | ||
[[Category: | [[Category: Mesecar AD]] | ||
[[Category: | [[Category: Pegan S]] | ||
[[Category: | [[Category: Serrano H]] | ||
[[Category: | [[Category: Whitman CP]] | ||
Latest revision as of 16:04, 30 August 2023
Structural and mechanistic analysis of trans-3-chloroacrylic acid dehalogenase activityStructural and mechanistic analysis of trans-3-chloroacrylic acid dehalogenase activity
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTrans-3-chloroacrylic acid dehalogenase (CaaD) is a critical enzyme in the trans-1,3-dichloropropene (DCP) degradation pathway in Pseudomonas pavonaceae 170. This enzyme allows bacteria to use trans-DCP, a common component in commercially produced fumigants, as a carbon source. CaaD specifically catalyzes the fourth step of the pathway by cofactor-independent dehalogenation of a vinyl carbon-halogen bond. Previous studies have reported an X-ray structure of CaaD under acidic conditions with a covalent modification of the catalytic betaPro1 residue. Here, the 1.7 A resolution X-ray structure of CaaD under neutral (pH 6.5) conditions is reported without the presence of the covalent adduct. In this new structure, a substrate-like acetate molecule is bound within the active site in a position analogous to the putative substrate-binding site. Additionally, a catalytically important water molecule was identified, consistent with previously proposed reaction schemes. Finally, flexibility of the catalytically relevant side chain alphaGlu52 is observed in the structure, supporting its role in the catalytic mechanism. Structural and mechanistic analysis of trans-3-chloroacrylic acid dehalogenase activity.,Pegan SD, Serrano H, Whitman CP, Mesecar AD Acta Crystallogr D Biol Crystallogr. 2008 Dec;64(Pt 12):1277-82. Epub 2008, Nov 18. PMID:19018104[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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