3b2s
From Proteopedia
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|PDB= 3b2s |SIZE=350|CAPTION= <scene name='initialview01'>3b2s</scene>, resolution 1.92Å | |PDB= 3b2s |SIZE=350|CAPTION= <scene name='initialview01'>3b2s</scene>, resolution 1.92Å | ||
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A+452'>AC1</scene>, <scene name='pdbsite=AC2:Coa+Binding+Site+For+Residue+A+454'>AC2</scene>, <scene name='pdbsite=AC3:B2s+Binding+Site+For+Residue+A+455'>AC3</scene> and <scene name='pdbsite=AC4:Mpo+Binding+Site+For+Residue+A+456'>AC4</scene> | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A+452'>AC1</scene>, <scene name='pdbsite=AC2:Coa+Binding+Site+For+Residue+A+454'>AC2</scene>, <scene name='pdbsite=AC3:B2s+Binding+Site+For+Residue+A+455'>AC3</scene> and <scene name='pdbsite=AC4:Mpo+Binding+Site+For+Residue+A+456'>AC4</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=B2S:(3ALPHA,7ALPHA)-3,7,15-TRIHYDROXY-12,13-EPOXYTRICHOTHEC-9-EN-8-ONE'>B2S</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPO:3[N-MORPHOLINO]PROPANE+SULFONIC+ACID'>MPO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Tri101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5518 Gibberella zeae]) | |GENE= Tri101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5518 Gibberella zeae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2zba|2ZBA]], [[2rkt|2RKT]], [[2rkv|2RKV]], [[3b30|3B30]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b2s OCA], [http://www.ebi.ac.uk/pdbsum/3b2s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3b2s RCSB]</span> | ||
}} | }} | ||
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[[Category: Garvey, G S.]] | [[Category: Garvey, G S.]] | ||
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
| - | [[Category: B2S]] | ||
| - | [[Category: COA]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: MPO]] | ||
| - | [[Category: NA]] | ||
[[Category: acetyl coa]] | [[Category: acetyl coa]] | ||
[[Category: acetyltransferase]] | [[Category: acetyltransferase]] | ||
| Line 38: | Line 36: | ||
[[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 Mon Mar 31 05:22:32 2008'' |
Revision as of 02:22, 31 March 2008
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| , resolution 1.92Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | , , , , | ||||||
| Gene: | Tri101 (Gibberella zeae) | ||||||
| Related: | 2ZBA, 2RKT, 2RKV, 3B30
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Sructure of F. graminearum TRI101 complexed with Coenzyme A and Deoxynivalenol
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
3B2S is a Single protein structure of sequence from Gibberella zeae. 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
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