3mf8: Difference between revisions
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< | ==Crystal Structure of Native cis-CaaD== | ||
<StructureSection load='3mf8' size='340' side='right'caption='[[3mf8]], [[Resolution|resolution]] 2.01Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3mf8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Coryneform_bacterium Coryneform bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MF8 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3mf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mf8 OCA], [https://pdbe.org/3mf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mf8 RCSB], [https://www.ebi.ac.uk/pdbsum/3mf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mf8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6VPE5_9CORY Q6VPE5_9CORY] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The isomeric mixture of cis- and trans-1,3-dichloropropene constitutes the active component of a widely used nematocide known as Telone II(R). The mixture is processed by various soil bacteria to acetaldehyde through the 1,3-dichloropropene catabolic pathway. The pathway relies on an isomer-specific hydrolytic dehalogenation reaction catalyzed by cis- or trans-3-chloroacrylic acid dehalogenase, known respectively as cis-CaaD and CaaD. Previous sequence analysis and crystallographic studies of the native and covalently modified enzymes identified Pro-1, His-28, Arg-70, Arg-73, Tyr-103, and Glu-114 as key binding and catalytic residues in cis-CaaD. Mutagenesis of these residues confirmed their importance to the dehalogenation reaction. Crystal structures of the native enzyme (2.01A resolution) and the enzyme covalently modified at the Pro-1 nitrogen by 2-hydroxypropanoate (1.65A resolution) are reported here. Both structures are at a resolution higher than previously reported (2.75A and 2.1A resolution, respectively). The conformation of the covalent adduct is strikingly different from that previously reported due to its interaction with a 7-residue loop (Thr-32 to Leu-38). The participation of another active site residue, Arg-117, in catalysis and inactivation was also examined. The implications of the combined findings for the mechanisms of catalysis and inactivation are discussed. | |||
Crystal structures of native and inactivated cis-3-chloroacrylic acid dehalogenase: Implications for the catalytic and inactivation mechanisms.,Guo Y, Serrano H, Johnson WH Jr, Ernst S, Hackert ML, Whitman CP Bioorg Chem. 2010 Oct 20. PMID:21074239<ref>PMID:21074239</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3mf8" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Dehalogenase 3D structures|Dehalogenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[ | |||
== | |||
< | |||
[[Category: Coryneform bacterium]] | [[Category: Coryneform bacterium]] | ||
[[Category: Ernst | [[Category: Large Structures]] | ||
[[Category: Guo | [[Category: Ernst SR]] | ||
[[Category: Hackert | [[Category: Guo Y]] | ||
[[Category: Johnson | [[Category: Hackert ML]] | ||
[[Category: Serrano | [[Category: Johnson Jr WH]] | ||
[[Category: Whitman | [[Category: Serrano H]] | ||
[[Category: Whitman CP]] | |||
Latest revision as of 11:52, 6 September 2023
Crystal Structure of Native cis-CaaDCrystal Structure of Native cis-CaaD
Structural highlights
FunctionPublication Abstract from PubMedThe isomeric mixture of cis- and trans-1,3-dichloropropene constitutes the active component of a widely used nematocide known as Telone II(R). The mixture is processed by various soil bacteria to acetaldehyde through the 1,3-dichloropropene catabolic pathway. The pathway relies on an isomer-specific hydrolytic dehalogenation reaction catalyzed by cis- or trans-3-chloroacrylic acid dehalogenase, known respectively as cis-CaaD and CaaD. Previous sequence analysis and crystallographic studies of the native and covalently modified enzymes identified Pro-1, His-28, Arg-70, Arg-73, Tyr-103, and Glu-114 as key binding and catalytic residues in cis-CaaD. Mutagenesis of these residues confirmed their importance to the dehalogenation reaction. Crystal structures of the native enzyme (2.01A resolution) and the enzyme covalently modified at the Pro-1 nitrogen by 2-hydroxypropanoate (1.65A resolution) are reported here. Both structures are at a resolution higher than previously reported (2.75A and 2.1A resolution, respectively). The conformation of the covalent adduct is strikingly different from that previously reported due to its interaction with a 7-residue loop (Thr-32 to Leu-38). The participation of another active site residue, Arg-117, in catalysis and inactivation was also examined. The implications of the combined findings for the mechanisms of catalysis and inactivation are discussed. Crystal structures of native and inactivated cis-3-chloroacrylic acid dehalogenase: Implications for the catalytic and inactivation mechanisms.,Guo Y, Serrano H, Johnson WH Jr, Ernst S, Hackert ML, Whitman CP Bioorg Chem. 2010 Oct 20. PMID:21074239[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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