1BCP
BINARY COMPLEX OF PERTUSSIS TOXIN AND ATP
Summary for 1BCP
| Entry DOI | 10.2210/pdb1bcp/pdb |
| Descriptor | PERTUSSIS TOXIN, ADENOSINE-5'-TRIPHOSPHATE, ... (7 entities in total) |
| Functional Keywords | toxin, adp-ribosyltransferase, transferase, whooping cough |
| Biological source | Bordetella pertussis More |
| Cellular location | Secreted: P04977 P04978 P04979 P0A3R5 P04981 |
| Total number of polymer chains | 12 |
| Total formula weight | 211371.73 |
| Authors | Hazes, B.,Read, R.J. (deposition date: 1995-11-21, release date: 1997-06-05, Last modification date: 2024-11-06) |
| Primary citation | Hazes, B.,Boodhoo, A.,Cockle, S.A.,Read, R.J. Crystal structure of the pertussis toxin-ATP complex: a molecular sensor. J.Mol.Biol., 258:661-671, 1996 Cited by PubMed 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. PubMed: 8637000DOI: 10.1006/jmbi.1996.0277 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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