1bcp
From Proteopedia
(New page: 200px<br /><applet load="1bcp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bcp, resolution 2.7Å" /> '''BINARY COMPLEX OF PER...) |
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| - | [[Image:1bcp.gif|left|200px]]<br /><applet load="1bcp" size=" | + | [[Image:1bcp.gif|left|200px]]<br /><applet load="1bcp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bcp, resolution 2.7Å" /> | caption="1bcp, resolution 2.7Å" /> | ||
'''BINARY COMPLEX OF PERTUSSIS TOXIN AND ATP'''<br /> | '''BINARY COMPLEX OF PERTUSSIS TOXIN AND ATP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Pertussis toxin is a major virulence factor of Bordetella pertussis, the | + | Pertussis toxin is a major virulence factor of Bordetella pertussis, the causative agent of whooping cough. The protein is a hexamer containing a catalytic subunit (S1) that is tightly associated with a pentameric cell-binding component (B-oligomer). In vitro experiments have shown that ATP and a number of detergents and phospholipids assist in activating the holotoxin by destabilizing the interaction between S1 and the B-oligomer. Similar processes may play a role in the activation of pertussis toxin in vivo. In this paper we present the crystal structure of the pertussis toxin-ATP complex and discuss the structural basis for the ATP-induced activation. In addition, we propose a physiological role for the ATP effect in the process by which the toxin enters the cytoplasm of eukaryotic cells. The key features of this proposal are that ATP binding signals the arrival of the toxin in the endoplasmic reticulum and, at the same time, triggers dissociation of the holotoxin prior to membrane translocation. |
==About this Structure== | ==About this Structure== | ||
| - | 1BCP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis] with ATP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1BCP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis] with <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Hazes, B.]] | [[Category: Hazes, B.]] | ||
| - | [[Category: Read, R | + | [[Category: Read, R J.]] |
[[Category: ATP]] | [[Category: ATP]] | ||
[[Category: adp-ribosyltransferase]] | [[Category: adp-ribosyltransferase]] | ||
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[[Category: whooping cough]] | [[Category: whooping cough]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:55 2008'' |
Revision as of 09:53, 21 February 2008
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BINARY COMPLEX OF PERTUSSIS TOXIN AND ATP
Overview
Pertussis toxin is a major virulence factor of Bordetella pertussis, the causative agent of whooping cough. The protein is a hexamer containing a catalytic subunit (S1) that is tightly associated with a pentameric cell-binding component (B-oligomer). In vitro experiments have shown that ATP and a number of detergents and phospholipids assist in activating the holotoxin by destabilizing the interaction between S1 and the B-oligomer. Similar processes may play a role in the activation of pertussis toxin in vivo. In this paper we present the crystal structure of the pertussis toxin-ATP complex and discuss the structural basis for the ATP-induced activation. In addition, we propose a physiological role for the ATP effect in the process by which the toxin enters the cytoplasm of eukaryotic cells. The key features of this proposal are that ATP binding signals the arrival of the toxin in the endoplasmic reticulum and, at the same time, triggers dissociation of the holotoxin prior to membrane translocation.
About this Structure
1BCP is a Protein complex structure of sequences from Bordetella pertussis with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the pertussis toxin-ATP complex: a molecular sensor., Hazes B, Boodhoo A, Cockle SA, Read RJ, J Mol Biol. 1996 May 17;258(4):661-71. PMID:8637000
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