2qk7: Difference between revisions

Revision as of 04:54, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2qk7.png

Template:STRUCTURE 2qk7

A covalent S-F heterodimer of staphylococcal gamma-hemolysinA covalent S-F heterodimer of staphylococcal gamma-hemolysin

Template:ABSTRACT PUBMED 18214982

About this StructureAbout this Structure

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

ReferenceReference

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

Engineered covalent leucotoxin heterodimers form functional pores: insights into S-F interactions., Joubert O, Viero G, Keller D, Martinez E, Colin DA, Monteil H, Mourey L, Dalla Serra M, Prevost G, Biochem J. 2006 Jun 1;396(2):381-9. PMID:16494579

Page seeded by OCA on Tue Jul 29 04:54:10 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2qk7|  PDB=2qk7  |  SCENE=  }}
-'''A covalent S-F heterodimer of staphylococcal gamma-hemolysin'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18214982}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18214982 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18214982}}
 ==About this Structure==
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 ==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://www.ncbi.nlm.nih.gov/pubmed/18214982 18214982]
+Engineered covalent leucotoxin heterodimers form functional pores: insights into S-F interactions., Joubert O, Viero G, Keller D, Martinez E, Colin DA, Monteil H, Mourey L, Dalla Serra M, Prevost G, Biochem J. 2006 Jun 1;396(2):381-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16494579 16494579]
 [[Category: Protein complex]]
 [[Category: Staphylococcus aureus]]
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 [[Category: Protein-protein interaction]]
 [[Category: Secreted]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:54:10 2008''