Abstract:
: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.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Hazes B,Boodhoo A,Cockle SA,Read RJdoi
10.1006/jmbi.1996.0277subject
Has Abstractpub_date
1996-05-17 00:00:00pages
661-71issue
4eissn
0022-2836issn
1089-8638pii
S0022-2836(96)90277-6journal_volume
258pub_type
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