2zba
From Proteopedia
(New page: 200px<br /><applet load="2zba" size="350" color="white" frame="true" align="right" spinBox="true" caption="2zba, resolution 2.00Å" /> '''Crystal Sructure of ...) |
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caption="2zba, resolution 2.00Å" /> | caption="2zba, resolution 2.00Å" /> | ||
'''Crystal Sructure of F. sporotrichioides TRI101 complexed with Coenzyme A and T-2'''<br /> | '''Crystal Sructure of F. sporotrichioides TRI101 complexed with Coenzyme A and T-2'''<br /> | ||
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| + | ==Overview== | ||
| + | Fusarium head blight (FHB) is a plant disease with serious economic and, health impacts. It is caused by fungal species belonging to the genus, Fusarium and the mycotoxins they produce. Although it has proved difficult, to combat this disease, one strategy that has been examined is the, introduction of an indigenous fungal protective gene into cereals such as, wheat barley and rice. Thus far the gene of choice has been tri101 whose, gene product catalyzes the transfer of an acetyl group from acetyl, coenzyme A to the C3 hydroxyl moiety of several trichothecene mycotoxins., In vitro this has been shown to reduce the toxicity of the toxins by, approximately 100-fold but has demonstrated limited resistance to FHB in, transgenic cereal. To understand the molecular basis for the differences, between in vitro and in vivo resistance the three-dimensional structures, and kinetic properties of two TRI101 orthologs isolated from Fusarium, sporotrichioides and Fusarium graminearum have been determined. The, kinetic results reveal important differences in activity of these enzymes, toward B-type trichothecenes such as deoxynivalenol. These differences in, activity can be explained in part by the three-dimensional structures for, the ternary complexes for both of these enzymes with coenzyme A and, trichothecene mycotoxins. The structural and kinetic results together, emphasize that the choice of an enzymatic resistance gene in transgenic, crop protection strategies must take into account the kinetic profile of, the selected protein. | ||
==About this Structure== | ==About this Structure== | ||
| - | 2ZBA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_sporotrichioides Fusarium sporotrichioides] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=COA:'>COA</scene>, <scene name='pdbligand=ZBA:'>ZBA</scene>, <scene name='pdbligand=DMS:'>DMS</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZBA OCA]. | + | 2ZBA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_sporotrichioides Fusarium sporotrichioides] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=COA:'>COA</scene>, <scene name='pdbligand=ZBA:'>ZBA</scene>, <scene name='pdbligand=DMS:'>DMS</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Ca Binding Site For Residue A 460'>AC1</scene>, <scene name='pdbsite=AC2:Ca Binding Site For Residue A 461'>AC2</scene>, <scene name='pdbsite=AC3:Coa Binding Site For Residue A 462'>AC3</scene>, <scene name='pdbsite=AC4:Coa Binding Site For Residue B 460'>AC4</scene>, <scene name='pdbsite=AC5:Coa Binding Site For Residue C 460'>AC5</scene>, <scene name='pdbsite=AC6:Coa Binding Site For Residue D 460'>AC6</scene>, <scene name='pdbsite=AC7:Zba Binding Site For Residue A 463'>AC7</scene>, <scene name='pdbsite=AC8:Zba Binding Site For Residue C 461'>AC8</scene>, <scene name='pdbsite=AC9:Zba Binding Site For Residue B 461'>AC9</scene>, <scene name='pdbsite=BC1:Zba Binding Site For Residue D 461'>BC1</scene>, <scene name='pdbsite=BC2:Dms Binding Site For Residue B 462'>BC2</scene> and <scene name='pdbsite=BC3:Gol Binding Site For Residue C 462'>BC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZBA OCA]. |
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| + | ==Reference== | ||
| + | Structural and functional characterization of the TRI101 trichothecene 3-O-acetyltransferase from Fusarium sporotrichioides and Fusarium graminearum: kinetic insights to combating Fusarium head blight., Garvey GS, McCormick SP, Rayment I, J Biol Chem. 2008 Jan 18;283(3):1660-9. Epub 2007 Oct 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17923480 17923480] | ||
[[Category: Fusarium sporotrichioides]] | [[Category: Fusarium sporotrichioides]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: trichothecene]] | [[Category: trichothecene]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 11:01:30 2008'' |
Revision as of 09:01, 31 January 2008
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Crystal Sructure of F. sporotrichioides TRI101 complexed with Coenzyme A and T-2
Overview
Fusarium head blight (FHB) is a plant disease with serious economic and, health impacts. It is caused by fungal species belonging to the genus, Fusarium and the mycotoxins they produce. Although it has proved difficult, to combat this disease, one strategy that has been examined is the, introduction of an indigenous fungal protective gene into cereals such as, wheat barley and rice. Thus far the gene of choice has been tri101 whose, gene product catalyzes the transfer of an acetyl group from acetyl, coenzyme A to the C3 hydroxyl moiety of several trichothecene mycotoxins., In vitro this has been shown to reduce the toxicity of the toxins by, approximately 100-fold but has demonstrated limited resistance to FHB in, transgenic cereal. To understand the molecular basis for the differences, between in vitro and in vivo resistance the three-dimensional structures, and kinetic properties of two TRI101 orthologs isolated from Fusarium, sporotrichioides and Fusarium graminearum have been determined. The, kinetic results reveal important differences in activity of these enzymes, toward B-type trichothecenes such as deoxynivalenol. These differences in, activity can be explained in part by the three-dimensional structures for, the ternary complexes for both of these enzymes with coenzyme A and, trichothecene mycotoxins. The structural and kinetic results together, emphasize that the choice of an enzymatic resistance gene in transgenic, crop protection strategies must take into account the kinetic profile of, the selected protein.
About this Structure
2ZBA is a Single protein structure of sequence from Fusarium sporotrichioides with , , , and as ligands. Known structural/functional Sites: , , , , , , , , , , and . Full crystallographic information is available from OCA.
Reference
Structural and functional characterization of the TRI101 trichothecene 3-O-acetyltransferase from Fusarium sporotrichioides and Fusarium graminearum: kinetic insights to combating Fusarium head blight., Garvey GS, McCormick SP, Rayment I, J Biol Chem. 2008 Jan 18;283(3):1660-9. Epub 2007 Oct 8. PMID:17923480
Page seeded by OCA on Thu Jan 31 11:01:30 2008
Categories: Fusarium sporotrichioides | Single protein | Garvey, G.S. | McCormick, S.P. | Rayment, I. | CA | COA | DMS | GOL | ZBA | Acetyl coa | Acetyltransferase | Bahd superfamily | Deoxynivalenol | Fusarium | T-2 | Tri101 | Trichothecene
