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.


1vcy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vcy.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1vcy.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1vcy| PDB=1vcy | SCENE= }}
{{STRUCTURE_1vcy| PDB=1vcy | SCENE= }}
-
'''VVA2 isoform'''
+
===VVA2 isoform===
-
==Overview==
+
<!--
-
Membrane adhesion and insertion of protein are essential to all organisms, but the underlying mechanisms remain largely unknown. Membrane pore-forming toxins (PFTs) are potential model systems for studying these mechanisms. We have determined the crystal structures of volvatoxin A2 (VVA2), a fungal PFT from Volvariella volvacea, using Br-multiple-wavelength anomalous diffraction (MAD). The VVA2 structures obtained at pH 4.6, pH 5.5 and pH 6.5 were refined to resolutions of 1.42 A, 2.6 A and 3.2 A, respectively. The structures reveal that the VVA2 monomer contains a single alpha/beta domain. Most of the VVA2 surface is occupied by its oligomerization motif and two putative heparin-binding motifs. Residues Ala91 to Ala101 display several conformations at different pH values, which might be under the control of His87. We also found that the shape of one putative heparin-binding motif in VVA2 appears similar to those found in fibroblast growth factors, and the other one displays a linear polypeptide. Our results suggest several possible intermediates of protein assembly in solution and protein adhering to cell membranes before conformational changes. The electron micrographs of VVA2 molecules in solution, at a protein concentration of 1 microg ml(-1), show that they can assemble into filament-like or braid-like oligomers in a pH-dependent way. In addition, the arc-shaped VVA2 structure obtained at pH 6.5 suggests that VVA2 could form a two-layered helical oligomer with 18 subunits per turn. The structures presented here could be used to elucidate the pore-formation mechanisms of VVA2 and its structural neighbors, Cyt toxins from Bacillus thuringiensis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15451675}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15451675 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15451675}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Lo, Y C.]]
[[Category: Lo, Y C.]]
[[Category: Toxin]]
[[Category: Toxin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:23:27 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:43:38 2008''

Revision as of 00:43, 28 July 2008

Image:1vcy.png

Template:STRUCTURE 1vcy

VVA2 isoform

Template:ABSTRACT PUBMED 15451675

About this Structure

Full crystallographic information is available from OCA.

Reference

Crystal structures and electron micrographs of fungal volvatoxin A2., Lin SC, Lo YC, Lin JY, Liaw YC, J Mol Biol. 2004 Oct 15;343(2):477-91. PMID:15451675

Page seeded by OCA on Mon Jul 28 03:43:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vcy"
Personal tools