1RWR

Crystal structure of filamentous hemagglutinin secretion domain

Summary for 1RWR

• Entry DOI: 10.2210/pdb1rwr/pdb
• Descriptor: Filamentous hemagglutinin (2 entities in total)
• Functional Keywords: type v secretion, beta-helix, adhesins, filamentous hemagglutinin, tps domain, cell adhesion
• Biological source: Bordetella pertussis
• Cellular location: Cell surface: P12255
• Total number of polymer chains: 1
• Total formula weight: 29719.27

Authors

Clantin, B.,Villeret, V. (deposition date: 2003-12-17, release date: 2004-04-13, Last modification date: 2024-03-13)

Primary citation

Clantin, B.,Hodak, H.,Willery, E.,Locht, C.,Jacob-Dubuisson, F.,Villeret, V.
The crystal structure of filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway
Proc.Natl.Acad.Sci.USA, 101:6194-6199, 2004

PubMed Abstract: 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.

PubMed: 15079085
DOI: 10.1073/pnas.0400291101

Experimental method

X-RAY DIFFRACTION (1.72 Å)