1bcp

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[[Image:1bcp.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bcp OCA], [http://www.ebi.ac.uk/pdbsum/1bcp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bcp RCSB]</span>
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'''BINARY COMPLEX OF PERTUSSIS TOXIN AND ATP'''
'''BINARY COMPLEX OF PERTUSSIS TOXIN AND ATP'''
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[[Category: Hazes, B.]]
[[Category: Hazes, B.]]
[[Category: Read, R J.]]
[[Category: Read, R J.]]
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[[Category: adp-ribosyltransferase]]
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[[Category: Adp-ribosyltransferase]]
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[[Category: toxin]]
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[[Category: Toxin]]
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[[Category: transferase]]
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[[Category: Transferase]]
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[[Category: whooping cough]]
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[[Category: Whooping cough]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:20:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:58:15 2008''
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Revision as of 08:20, 2 May 2008

Template:STRUCTURE 1bcp

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. 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 Page seeded by OCA on Fri May 2 11:20:54 2008

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