3mf8: Difference between revisions
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==Crystal Structure of Native cis-CaaD== | ==Crystal Structure of Native cis-CaaD== | ||
<StructureSection load='3mf8' size='340' side='right' caption='[[3mf8]], [[Resolution|resolution]] 2.01Å' scene=''> | <StructureSection load='3mf8' size='340' side='right' caption='[[3mf8]], [[Resolution|resolution]] 2.01Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mf7|3mf7]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mf7|3mf7]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cis-caaD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1728 coryneform bacterium])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cis-caaD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1728 coryneform bacterium])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mf8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mf8 RCSB], [http://www.ebi.ac.uk/pdbsum/3mf8 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mf8 OCA], [http://pdbe.org/3mf8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mf8 RCSB], [http://www.ebi.ac.uk/pdbsum/3mf8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mf8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3mf8" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 03:46, 5 August 2016
Crystal Structure of Native cis-CaaDCrystal Structure of Native cis-CaaD
Structural highlights
Publication 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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