1dab | pdb_00001dab
The Structure of Bordetella Pertussis Virulence Factor P.69 Pertactin
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Overview
A new generation of whooping-cough vaccines contain P.69 pertactin, a, surface-exposed domain of an outer membrane protein expressed by the, virulent bacterium Bordetella pertussis. This protein is a virulence, factor that mediates adhesion to target mammalian cells, a reaction that, is in part mediated by an RGD sequence. The X-ray crystal structure of, P.69 pertactin has been determined to 2.5 A. The protein fold consists of, a 16-stranded parallel beta-helix with a V-shaped cross-section, and is, the largest beta-helix known to date. Several between-strand weakly, conserved amino-acid repeats form internal and external ladders. The, structure appears as a helix from which several loops protrude, which, contain sequence motifs associated with the biological activity of the, protein. One particular (GGXXP)5 sequence is located directly after the, RGD motif, and may mediate interaction with epithelial cells. The, carboxy-terminal region of P.69 pertactin incorporates a (PQP)5 motif loop, containing the major immunoprotective epitope.
About this Structure
1DAB is a Single protein structure of sequence from Bordetella pertussis. Full crystallographic information is available from OCA.
Reference
Structure of Bordetella pertussis virulence factor P.69 pertactin., Emsley P, Charles IG, Fairweather NF, Isaacs NW, Nature. 1996 May 2;381(6577):90-2. PMID:8609998
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