3ej9: Difference between revisions
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==Structural and mechanistic analysis of trans-3-chloroacrylic acid dehalogenase activity== | ==Structural and mechanistic analysis of trans-3-chloroacrylic acid dehalogenase activity== | ||
<StructureSection load='3ej9' size='340' side='right' caption='[[3ej9]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='3ej9' size='340' side='right'caption='[[3ej9]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ej9]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3ej9]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/"pseudomonas_pavonaceae"_levine_and_soppeland_1926 "pseudomonas pavonaceae" levine and soppeland 1926]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EJ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EJ9 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ej3|3ej3]], [[3ej7|3ej7]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ej3|3ej3]], [[3ej7|3ej7]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">caaD1 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">caaD1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=47881 "Pseudomonas pavonaceae" Levine and Soppeland 1926]), caaD2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=47881 "Pseudomonas pavonaceae" Levine and Soppeland 1926])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ej9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ej9 OCA], [https://pdbe.org/3ej9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ej9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ej9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ej9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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==See Also== | ==See Also== | ||
*[[Dehalogenase|Dehalogenase]] | *[[Dehalogenase 3D structures|Dehalogenase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Pseudomonas pavonaceae levine and soppeland 1926]] | [[Category: Pseudomonas pavonaceae levine and soppeland 1926]] | ||
[[Category: Large Structures]] | |||
[[Category: Mesecar, A D]] | [[Category: Mesecar, A D]] | ||
[[Category: Pegan, S]] | [[Category: Pegan, S]] | ||
Revision as of 22:41, 20 October 2021
Structural and mechanistic analysis of trans-3-chloroacrylic acid dehalogenase activityStructural and mechanistic analysis of trans-3-chloroacrylic acid dehalogenase activity
Structural highlights
Evolutionary 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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