D
IPR027439

Protective antigen, heptamerisation domain

InterPro entry
Short namePA_heptamer_dom
Overlapping
homologous
superfamilies
 

Description

This entry represents pat of domain 2 of PA and similar proteins from firmicutes.

Protective antigen (PA) is the central component of the three-part protein toxin secreted by Bacillus anthracis, the organism responsible for anthrax. Homologues of PA have been found in several spore-forming Gram-positive bacteria, and share the ability to translocate toxic enzymes into the host cytosol. The PA monomer is organised mainly into antiparallel β-sheets and has four domains: an N-terminal domain (domain 1,
IPR011658
) containing two calcium ions and the cleavage site for activating proteases; a heptamerisation domain (domain 2,
IPR035088
and
IPR027439
) containing a large flexible loop implicated in membrane insertion; a small domain with several key residues for oligomerisation (domain 3,
IPR035331
); and a C-terminal receptor-binding domain (domain 4,
IPR048853
)
[1, 2, 4, 3]
.

References

1.Crystal structure of the anthrax toxin protective antigen. Petosa C, Collier RJ, Klimpel KR, Leppla SH, Liddington RC. Nature 385, 833-8, (1997). View articlePMID: 9039918

2.Structure of heptameric protective antigen bound to an anthrax toxin receptor: a role for receptor in pH-dependent pore formation. Lacy DB, Wigelsworth DJ, Melnyk RA, Harrison SC, Collier RJ. Proc. Natl. Acad. Sci. U.S.A. 101, 13147-51, (2004). View articlePMID: 15326297

3.Identification of a receptor-binding region within domain 4 of the protective antigen component of anthrax toxin. Varughese M, Teixeira AV, Liu S, Leppla SH. Infect Immun 67, 1860-5, (1999). View articlePMID: 10085028

4.Involvement of domain 3 in oligomerization by the protective antigen moiety of anthrax toxin. Mogridge J, Mourez M, Collier RJ. J Bacteriol 183, 2111-6, (2001). View articlePMID: 11222612

GO terms

molecular function

  • None

cellular component

  • None
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