Abstract:
:Helicobacter pylori secretes a unique virulence factor, Tipalpha, that enters gastric cells and both stimulates the production of the TNF-alpha and activates the NF-kappaB pathway. The structures of a truncated version of Tipalpha (TipalphaN34) in two crystal forms are presented here. Tipalpha adopts a novel beta(1)alpha(1)alpha(2)beta(2)beta(3)alpha(3)alpha(4) topology that can be described as a combination of three domains. A first region consists in a short flexible extension, a second displays a dodecin-like fold and a third is a helical bundle domain similar to the sterile alpha motif (SAM). Analysis of the oligomerisation states of TipalphaN34 in the crystals and in solution suggests that the disulfide bridges could hold together Tipalpha monomers during their secretion in the gastric environment.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Tosi T,Cioci G,Jouravleva K,Dian C,Terradot Ldoi
10.1016/j.febslet.2009.04.033subject
Has Abstractpub_date
2009-05-19 00:00:00pages
1581-5issue
10eissn
0014-5793issn
1873-3468pii
S0014-5793(09)00325-1journal_volume
583pub_type
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