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| | <StructureSection load='1wcg' size='340' side='right'caption='[[1wcg]], [[Resolution|resolution]] 1.10Å' scene=''> | | <StructureSection load='1wcg' size='340' side='right'caption='[[1wcg]], [[Resolution|resolution]] 1.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1wcg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brebr Brebr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WCG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1wcg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevicoryne_brassicae Brevicoryne brassicae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WCG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thioglucosidase Thioglucosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.147 3.2.1.147] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=1wcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wcg OCA], [https://pdbe.org/1wcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wcg RCSB], [https://www.ebi.ac.uk/pdbsum/1wcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wcg 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=1wcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wcg OCA], [https://pdbe.org/1wcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wcg RCSB], [https://www.ebi.ac.uk/pdbsum/1wcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wcg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MYRO1_BREBR MYRO1_BREBR]] Hydrolyzes glucosinolates to a labile aglycone. This rapidly undergoes spontaneous rearrangement, eliminating sulfur to yield a number of toxic metabolites. Thereby developing a chemical defense system that exploits and mimics the host plant.<ref>PMID:11804799</ref> <ref>PMID:17623639</ref>
| + | [https://www.uniprot.org/uniprot/MYRO1_BREBR MYRO1_BREBR] Hydrolyzes glucosinolates to a labile aglycone. This rapidly undergoes spontaneous rearrangement, eliminating sulfur to yield a number of toxic metabolites. Thereby developing a chemical defense system that exploits and mimics the host plant.<ref>PMID:11804799</ref> <ref>PMID:17623639</ref> |
| | == 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: Brebr]] | + | [[Category: Brevicoryne brassicae]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thioglucosidase]]
| + | [[Category: Arzt S]] |
| - | [[Category: Arzt, S]] | + | [[Category: Bones AM]] |
| - | [[Category: Bones, A M]] | + | [[Category: Brandt A]] |
| - | [[Category: Brandt, A]] | + | [[Category: Burmeister WP]] |
| - | [[Category: Burmeister, W P]] | + | [[Category: Haertel FV]] |
| - | [[Category: Haertel, F V]] | + | [[Category: Husebye H]] |
| - | [[Category: Husebye, H]] | + | [[Category: Rossiter JT]] |
| - | [[Category: Rossiter, J T]] | + | |
| - | [[Category: Aphid]]
| + | |
| - | [[Category: Beta-barrel]]
| + | |
| - | [[Category: Beta-glucosidase]]
| + | |
| - | [[Category: Glucosidase]]
| + | |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Insect]]
| + | |
| - | [[Category: Myrosinase]]
| + | |
| Structural highlights
Function
MYRO1_BREBR Hydrolyzes glucosinolates to a labile aglycone. This rapidly undergoes spontaneous rearrangement, eliminating sulfur to yield a number of toxic metabolites. Thereby developing a chemical defense system that exploits and mimics the host plant.[1] [2]
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 PubMed
The aphid Brevicoryne brassicae is a specialist feeding on Brassicaceae plants. The insect has an intricate defence system involving a beta-D-thioglucosidase (myrosinase) that hydrolyses glucosinolates sequestered from the host plant into volatile isothiocyanates. These isothiocyanates act synergistically with the pheromone E-beta-farnesene to form an alarm system when the aphid is predated. In order to investigate the enzymatic characteristics of the aphid myrosinase and its three-dimensional structure, milligram amounts of pure recombinant aphid myrosinase were obtained from Echerichia coli. The recombinant enzyme had similar physiochemical properties to the native enzyme. The global structure is very similar to Sinapis alba myrosinase and plant beta-O-glucosidases. Aphid myrosinase has two catalytic glutamic acid residues positioned as in plant beta-O-glucosidases, and it is not obvious why this unusual enzyme hydrolyses glucosinolates, the common substrates of plant myrosinases which are normally not hydrolyzed by plant beta-O-glucosidases. The only residue specific for aphid myrosinase in proximity of the glycosidic linkage is Tyr180 which may have a catalytic role. The aglycon binding site differs strongly from plant myrosinase, whereas due to the presence of Trp424 in the glucose binding site, this part of the active site is more similar to plant beta-O-glucosidases, as plant myrosinases carry a phenylalanine residue at this position.
Crystal structure at 1.1 Angstroms resolution of an insect myrosinase from Brevicoryne brassicae shows its close relationship to beta-glucosidases.,Husebye H, Arzt S, Burmeister WP, Hartel FV, Brandt A, Rossiter JT, Bones AM Insect Biochem Mol Biol. 2005 Dec;35(12):1311-20. Epub 2005 Aug 18. PMID:16291087[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jones AM, Winge P, Bones AM, Cole R, Rossiter JT. Characterization and evolution of a myrosinase from the cabbage aphid Brevicoryne brassicae. Insect Biochem Mol Biol. 2002 Mar 1;32(3):275-84. PMID:11804799
- ↑ Kazana E, Pope TW, Tibbles L, Bridges M, Pickett JA, Bones AM, Powell G, Rossiter JT. The cabbage aphid: a walking mustard oil bomb. Proc Biol Sci. 2007 Sep 22;274(1623):2271-7. PMID:17623639 doi:http://dx.doi.org/10.1098/rspb.2007.0237
- ↑ Husebye H, Arzt S, Burmeister WP, Hartel FV, Brandt A, Rossiter JT, Bones AM. Crystal structure at 1.1 Angstroms resolution of an insect myrosinase from Brevicoryne brassicae shows its close relationship to beta-glucosidases. Insect Biochem Mol Biol. 2005 Dec;35(12):1311-20. Epub 2005 Aug 18. PMID:16291087 doi:http://dx.doi.org/10.1016/j.ibmb.2005.07.004
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