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New page: left|200px<br /> <applet load="1wcg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wcg, resolution 1.10Å" /> '''APHID MYROSINASE'''... |
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== | ==Aphid myrosinase== | ||
The aphid Brevicoryne brassicae is a specialist feeding on Brassicaceae | <StructureSection load='1wcg' size='340' side='right'caption='[[1wcg]], [[Resolution|resolution]] 1.10Å' scene=''> | ||
== Structural highlights == | |||
<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='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='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> | |||
</table> | |||
== 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> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wc/1wcg_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wcg ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:16291087</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1wcg" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Brevicoryne brassicae]] | [[Category: Brevicoryne brassicae]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Arzt | [[Category: Arzt S]] | ||
[[Category: Bones | [[Category: Bones AM]] | ||
[[Category: Brandt | [[Category: Brandt A]] | ||
[[Category: Burmeister | [[Category: Burmeister WP]] | ||
[[Category: Haertel | [[Category: Haertel FV]] | ||
[[Category: Husebye | [[Category: Husebye H]] | ||
[[Category: Rossiter | [[Category: Rossiter JT]] | ||
Latest revision as of 16:28, 13 December 2023
Aphid myrosinaseAphid myrosinase
Structural highlights
FunctionMYRO1_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 PubMedThe 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
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