1rwr
From Proteopedia
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Crystal structure of filamentous hemagglutinin secretion domain
Overview
Filamentous hemagglutinin (FHA), the major 230-kDa adhesin of the whooping, cough agent Bordetella pertussis, is one of the most efficiently secreted, proteins in Gram-negative bacteria. FHA is secreted by means of the, two-partner secretion (TPS) pathway. Several important human, animal, and, plant pathogens also secrete adhesins and other virulence factors by using, this mode of secretion. A TPS system is composed of two separate proteins, with TpsA the secreted protein and TpsB its associated specific, outermembrane transporter. All TPS-secreted proteins contain a distinctive, N-proximal module essential for secretion, the TPS domain. We report here, the 1.7- A structure of a functionally secreted 30-kDa N-terminal fragment, of FHA. It reveals that the TPS domain folds into a beta-helix, with three, extrahelical motifs, a beta-hairpin, a four-stranded beta-sheet, and an, N-terminal capping, mostly formed by the nonconserved regions of the TPS, domain. The structure thus explains why the TPS domain is able to initiate, folding of the beta-helical motifs that form the central domain of the, adhesin, because it is itself a beta-helical scaffold. It also contains, less conserved extrahelical regions most likely involved in specific, properties, such as the recognition of the outer-membrane transporter., This structure is representative of the TPS domains found so far in >100, secreted proteins from pathogenic bacteria. It also provides a mechanistic, insight into how protein folding may be linked to secretion in the TPS, pathway.
About this Structure
1RWR is a Single protein structure of sequence from Bordetella pertussis. Full crystallographic information is available from OCA.
Reference
The crystal structure of filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway., Clantin B, Hodak H, Willery E, Locht C, Jacob-Dubuisson F, Villeret V, Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):6194-9. Epub 2004 Apr 12. PMID:15079085
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