1PRT

THE CRYSTAL STRUCTURE OF PERTUSSIS TOXIN

Summary for 1PRT

• Entry DOI: 10.2210/pdb1prt/pdb
• Descriptor: PERTUSSIS TOXIN (SUBUNIT S1), PERTUSSIS TOXIN (SUBUNIT S2), PERTUSSIS TOXIN (SUBUNIT S3), ... (5 entities in total)
• Functional Keywords: toxin
• Biological source: Bordetella pertussis; More
• Cellular location: Secreted: P04977 P04978 P04979 P0A3R5 P04981
• Total number of polymer chains: 12
• Total formula weight: 208907.85

Authors

Stein, P.E.,Read, R.J. (deposition date: 1993-11-22, release date: 1995-01-26, Last modification date: 2024-10-23)

Primary citation

Stein, P.E.,Boodhoo, A.,Armstrong, G.D.,Cockle, S.A.,Klein, M.H.,Read, R.J.
The crystal structure of pertussis toxin.
Structure, 2:45-57, 1994

PubMed Abstract: Pertussis toxin is an exotoxin of the A-B class produced by Bordetella pertussis. The holotoxin comprises 952 residues forming six subunits (five different sequences, S1-S5). It plays an important role in the development of protective immunity to whooping cough, and is an essential component of new acellular vaccines. It is also widely used as a biochemical tool to ADP-ribosylate GTP-binding proteins in the study of signal transduction.

PubMed: 8075982
DOI: 10.1016/S0969-2126(00)00007-1

Experimental method

X-RAY DIFFRACTION (2.9 Å)