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.


1kho

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kho.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1kho.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kho| PDB=1kho | SCENE= }}
{{STRUCTURE_1kho| PDB=1kho | SCENE= }}
-
'''Crystal Structure Analysis of Clostridium perfringens alpha-Toxin Isolated from Avian Strain SWCP'''
+
===Crystal Structure Analysis of Clostridium perfringens alpha-Toxin Isolated from Avian Strain SWCP===
-
==Overview==
+
<!--
-
Clostridium perfringens alpha-toxin is a 370-residue, zinc-dependent, phospholipase C that is the key virulence determinant in gas gangrene. It is also implicated in the pathogenesis of sudden death syndrome in young animals and necrotic enteritis in chickens. Previously characterized alpha-toxins from different strains of C. perfringens are almost identical in sequence and biochemical properties. We describe the cloning, nucleotide sequencing, expression, characterization, and crystal structure of alpha-toxin from an avian strain, SWan C. perfringens (SWCP), which has a large degree of sequence variation and altered substrate specificity compared to these strains. The structure of alpha-toxin from strain CER89L43 has been previously reported in open (active site accessible to substrate) and closed (active site obscured by loop movements) conformations. The SWCP structure is in an open-form conformation, with three zinc ions in the active site. This is the first example of an open form of alpha-toxin crystallizing without the addition of divalent cations to the crystallization buffer, indicating that the protein can retain three zinc ions bound in the active site. The topology of the calcium binding site formed by residues 269, 271, 336, and 337, which is essential for membrane binding, is significantly altered in comparison with both the open and closed alpha-toxin structures. We are able to relate these structural changes to the different substrate specificity and membrane binding properties of this divergent alpha-toxin. This will provide essential information when developing an effective vaccine that will protect against C. perfringens infection in a wide range of domestic livestock.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12009886}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12009886 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12009886}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: C-terminal beta-sheet]]
[[Category: C-terminal beta-sheet]]
[[Category: N-terminal alpha-helix]]
[[Category: N-terminal alpha-helix]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:45:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:21:37 2008''

Revision as of 07:21, 2 July 2008

Image:1kho.png

Template:STRUCTURE 1kho

Crystal Structure Analysis of Clostridium perfringens alpha-Toxin Isolated from Avian Strain SWCP

Template:ABSTRACT PUBMED 12009886

About this Structure

1KHO is a Single protein structure of sequence from Clostridium perfringens. Full crystallographic information is available from OCA.

Reference

The first strain of Clostridium perfringens isolated from an avian source has an alpha-toxin with divergent structural and kinetic properties., Justin N, Walker N, Bullifent HL, Songer G, Bueschel DM, Jost H, Naylor C, Miller J, Moss DS, Titball RW, Basak AK, Biochemistry. 2002 May 21;41(20):6253-62. PMID:12009886

Page seeded by OCA on Wed Jul 2 10:21:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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