2hgo
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2hgo.jpg|left|200px]] | + | [[Image:2hgo.jpg|left|200px]] |
| - | + | ||
| - | '''NMR structure of Cassiicolin''' | + | {{Structure |
| + | |PDB= 2hgo |SIZE=350|CAPTION= <scene name='initialview01'>2hgo</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=3HD:3-O-METHYL-O-ALPHA-D-MANNOPYRANOSYL'>3HD</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NMR structure of Cassiicolin''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2HGO is a [ | + | 2HGO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Corynespora_cassiicola Corynespora cassiicola]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HGO OCA]. |
==Reference== | ==Reference== | ||
| - | Structural analysis of cassiicolin, a host-selective protein toxin from Corynespora cassiicola., Barthe P, Pujade-Renaud V, Breton F, Gargani D, Thai R, Roumestand C, de Lamotte F, J Mol Biol. 2007 Mar 16;367(1):89-101. Epub 2006 Dec 5. PMID:[http:// | + | Structural analysis of cassiicolin, a host-selective protein toxin from Corynespora cassiicola., Barthe P, Pujade-Renaud V, Breton F, Gargani D, Thai R, Roumestand C, de Lamotte F, J Mol Biol. 2007 Mar 16;367(1):89-101. Epub 2006 Dec 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17234212 17234212] |
[[Category: Corynespora cassiicola]] | [[Category: Corynespora cassiicola]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 22: | Line 31: | ||
[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:16:51 2008'' |
Revision as of 15:16, 20 March 2008
| |||||||
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR structure of Cassiicolin
Overview
Cassiicolin is a host-selective toxin (HST) produced by the fungus Corynespora cassiicola (strain CCP). It is responsible for the Corynespora leaf fall (CLF) disease, which is among the main pathologies affecting rubber tree (Hevea brasiliensis). Working on purified cassiicolin and using electron microscopy, we have demonstrated that this 27-residue O-glycosylated protein is able to induce cellular damages identical to those induced by the fungus on rubber tree leaves and displays the same host selectivity. The solution structure and disulfide pairing of cassiicolin have been determined using NMR spectroscopy and simulated annealing calculations. Cassiicolin appears to have an original structure with a prolate ellipsoid shape. It adopts an over-all fold consisting of three strands arranged in a right-handed twisted, antiparallel beta-sheet knitted by three disulfide bonds. Its conformation resembles that found in small trypsine-like inhibitors isolated from the brain, the fat body and the hemolymph of locust grasshoppers. But cassiicolin has no sequence homology with these protease inhibitors, and lacks their characteristic substrate-binding loop. Probably, this motif represents one of the few highly stabilized "minimal" scaffolds, with a high sequence permissiveness, that nature has selected to evolve over different phyla and to support different functions. The knowledge of the 3D structure opens the way to the delineation of the mechanism of action of the toxin using site-directed mutagenesis.
About this Structure
2HGO is a Single protein structure of sequence from Corynespora cassiicola. Full crystallographic information is available from OCA.
Reference
Structural analysis of cassiicolin, a host-selective protein toxin from Corynespora cassiicola., Barthe P, Pujade-Renaud V, Breton F, Gargani D, Thai R, Roumestand C, de Lamotte F, J Mol Biol. 2007 Mar 16;367(1):89-101. Epub 2006 Dec 5. PMID:17234212
Page seeded by OCA on Thu Mar 20 17:16:51 2008
