We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1iaz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1iaz.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1iaz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1iaz| PDB=1iaz | SCENE= }}
{{STRUCTURE_1iaz| PDB=1iaz | SCENE= }}
-
'''EQUINATOXIN II'''
+
===EQUINATOXIN II===
-
==Overview==
+
<!--
-
BACKGROUND: Membrane pore-forming toxins have a remarkable property: they adopt a stable soluble form structure, which, when in contact with a membrane, undergoes a series of transformations, leading to an active, membrane-bound form. In contrast to bacterial toxins, no structure of a pore-forming toxin from an eukaryotic organism has been determined so far, an indication that structural studies of equinatoxin II (EqtII) may unravel a novel mechanism. RESULTS: The crystal structure of the soluble form of EqtII from the sea anemone Actinia equina has been determined at 1.9 A resolution. EqtII is shown to be a single-domain protein based on a 12 strand beta sandwich fold with a hydrophobic core and a pair of alpha helices, each of which is associated with the face of a beta sheet. CONCLUSIONS: The structure of the 30 N-terminal residues is the largest segment that can adopt a different structure without disrupting the fold of the beta sandwich core. This segment includes a three-turn alpha helix that lies on the surface of a beta sheet and ends in a stretch of three positively charged residues, Lys-30, Arg-31, and Lys-32. On the basis of gathered data, it is suggested that this segment forms the membrane pore, whereas the beta sandwich structure remains unaltered and attaches to a membrane as do other structurally related extrinsic membrane proteins or their domains. The use of a structural data site-directed mutagenesis study should reveal the residues involved in membrane pore formation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11525171}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11525171 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11525171}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Turk, D.]]
[[Category: Turk, D.]]
[[Category: Beta-sandwich]]
[[Category: Beta-sandwich]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:47:24 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:41:28 2008''

Revision as of 07:41, 1 July 2008

Image:1iaz.png

Template:STRUCTURE 1iaz

EQUINATOXIN II

Template:ABSTRACT PUBMED 11525171

About this Structure

1IAZ is a Single protein structure of sequence from Actinia equina. Full crystallographic information is available from OCA.

Reference

Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina., Athanasiadis A, Anderluh G, Macek P, Turk D, Structure. 2001 Apr 4;9(4):341-6. PMID:11525171

Page seeded by OCA on Tue Jul 1 10:41:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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