5c8z
From Proteopedia
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<StructureSection load='5c8z' size='340' side='right' caption='[[5c8z]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='5c8z' size='340' side='right' caption='[[5c8z]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5c8z]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C8Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C8Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5c8z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Biooc Biooc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C8Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C8Z FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZGR:2,4-DIHYDROXY-6-[(1E,10S)-10-HYDROXY-6-OXOUNDEC-1-EN-1-YL]BENZOIC+ACID'>ZGR</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZGR:2,4-DIHYDROXY-6-[(1E,10S)-10-HYDROXY-6-OXOUNDEC-1-EN-1-YL]BENZOIC+ACID'>ZGR</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c7y|5c7y]], [[5c81|5c81]], [[5c8x|5c8x]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c7y|5c7y]], [[5c81|5c81]], [[5c8x|5c8x]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">zhd101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29856 BIOOC])</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=5c8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c8z OCA], [http://pdbe.org/5c8z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c8z RCSB], [http://www.ebi.ac.uk/pdbsum/5c8z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c8z ProSAT]</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=5c8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c8z OCA], [http://pdbe.org/5c8z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c8z RCSB], [http://www.ebi.ac.uk/pdbsum/5c8z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c8z ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Zearalenone hydrolase (ZHD) is an alpha/beta-hydrolase that detoxifies and degrades the lactone zearalenone (ZEN), a naturally occurring oestrogenic mycotoxin that contaminates crops. Several apoenzyme and enzyme-substrate complex structures have been reported in the resolution range 2.4-2.6 A. However, the properties and mechanism of this enzyme are not yet fully understood. Here, a 1.60 A resolution structure of a ZHD-product complex is reported which was determined from a C-terminally His6-tagged ZHD crystal soaked with 2 mM ZEN for 30 min. It shows that after the lactone-bond cleavage, the phenol-ring region moves closer to residues Leu132, Tyr187 and Pro188, while the lactone-ring region barely moves. Comparisons of the ZHD-substrate and ZHD-product structures show that the hydrophilic interactions change, especially Trp183 N(1), which shifts from contacting O2 to O12', suggesting that Trp183 is responsible for the unidirectional translational movement of the phenol ring. This structure provides information on the final stage of the catalytic mechanism of zearalenone hydrolysis. | ||
| + | |||
| + | The structure of a complex of the lactonohydrolase zearalenone hydrolase with the hydrolysis product of zearalenone at 1.60 A resolution.,Qi Q, Yang WJ, Zhou HJ, Ming DM, Sun KL, Xu TY, Hu XJ, Lv H Acta Crystallogr F Struct Biol Commun. 2017 Jul 1;73(Pt 7):376-381. doi:, 10.1107/S2053230X17007713. Epub 2017 Jun 17. PMID:28695844<ref>PMID:28695844</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5c8z" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Biooc]] | ||
[[Category: Hu, X J]] | [[Category: Hu, X J]] | ||
[[Category: Qi, Q]] | [[Category: Qi, Q]] | ||
Revision as of 05:46, 25 April 2018
ZHD-ZGR complex after ZHD crystal soaking in ZEN for 30min
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