This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2hgo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2hgo.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2hgo.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2hgo| PDB=2hgo | SCENE= }}
{{STRUCTURE_2hgo| PDB=2hgo | SCENE= }}
-
'''NMR structure of Cassiicolin'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17234212}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17234212 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17234212}}
==About this Structure==
==About this Structure==
-
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].
+
2HGO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Corynespora_cassiicola Corynespora cassiicola]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HGO OCA].
==Reference==
==Reference==
Line 29: Line 33:
[[Category: Glycoprotein]]
[[Category: Glycoprotein]]
[[Category: Toxin]]
[[Category: Toxin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:16:22 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:00:21 2008''

Revision as of 04:00, 29 July 2008

Image:2hgo.png

Template:STRUCTURE 2hgo

NMR structure of Cassiicolin

Template:ABSTRACT PUBMED 17234212

About this Structure

2HGO is a Single protein structure of sequence from Corynespora cassiicola. Full experimental 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 Tue Jul 29 07:00:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hgo"
Personal tools