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.


2qk7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2qk7" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qk7, resolution 2.40&Aring;" /> '''A covalent S-F heter...)
Line 1: Line 1:
-
[[Image:2qk7.jpg|left|200px]]<br /><applet load="2qk7" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2qk7.jpg|left|200px]]
-
caption="2qk7, resolution 2.40&Aring;" />
+
 
-
'''A covalent S-F heterodimer of staphylococcal gamma-hemolysin'''<br />
+
{{Structure
 +
|PDB= 2qk7 |SIZE=350|CAPTION= <scene name='initialview01'>2qk7</scene>, resolution 2.40&Aring;
 +
|SITE=
 +
|LIGAND=
 +
|ACTIVITY=
 +
|GENE= hlgA, hlg2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]), hlgB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
 +
}}
 +
 
 +
'''A covalent S-F heterodimer of staphylococcal gamma-hemolysin'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2QK7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QK7 OCA].
+
2QK7 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QK7 OCA].
==Reference==
==Reference==
-
A covalent S-F heterodimer of leucotoxin reveals molecular plasticity of beta-barrel pore-forming toxins., Roblin P, Guillet V, Joubert O, Keller D, Erard M, Maveyraud L, Prevost G, Mourey L, Proteins. 2008 Jan 23;71(1):485-496. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18214982 18214982]
+
A covalent S-F heterodimer of leucotoxin reveals molecular plasticity of beta-barrel pore-forming toxins., Roblin P, Guillet V, Joubert O, Keller D, Erard M, Maveyraud L, Prevost G, Mourey L, Proteins. 2008 Jan 23;71(1):485-496. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18214982 18214982]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
Line 26: Line 35:
[[Category: secreted]]
[[Category: secreted]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:39:59 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:26:45 2008''

Revision as of 16:26, 20 March 2008


PDB ID 2qk7

Drag the structure with the mouse to rotate
, resolution 2.40Å
Gene: hlgA, hlg2 (Staphylococcus aureus), hlgB (Staphylococcus aureus)
Coordinates: save as pdb, mmCIF, xml



A covalent S-F heterodimer of staphylococcal gamma-hemolysin


Overview

Staphylococcal leucotoxins, leucocidins, and gamma-hemolysins are bicomponent beta-barrel pore-forming toxins (beta-PFTs). Their production is associated with several clinical diseases. They have cytotoxic activity due to the synergistic action of a class S component and a class F component, which are secreted as water-soluble monomers and form hetero-oligomeric transmembrane pores, causing the lysis of susceptible cells. Structural information is currently available for the monomeric S and F proteins and the homoheptamer formed by the related alpha-hemolysin. These structures illustrate the start and end points in the mechanistic framework of beta-PFT assembly. Only limited structural data exist for the intermediate stages, including hetero-oligomeric complexes of leucotoxins. We investigated the protein-protein interactions responsible for maintaining the final bipartite molecular architecture and describe here the high-resolution crystal structure and low-resolution solution structure of a site-specific cross-linked heterodimer of gamma-hemolysin (HlgA T28C-HlgB N156C), which were solved by X-ray crystallography and small angle X-ray scattering, respectively. These structures reveal a molecular plasticity of beta-PFTs, which may facilitate the transition from membrane-bound monomers to heterodimers. Proteins 2008. (c) 2008 Wiley-Liss, Inc.

About this Structure

2QK7 is a Protein complex structure of sequences from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

A covalent S-F heterodimer of leucotoxin reveals molecular plasticity of beta-barrel pore-forming toxins., Roblin P, Guillet V, Joubert O, Keller D, Erard M, Maveyraud L, Prevost G, Mourey L, Proteins. 2008 Jan 23;71(1):485-496. PMID:18214982

Page seeded by OCA on Thu Mar 20 18:26:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools