This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1rwr
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1rwr.gif|left|200px]] | [[Image:1rwr.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1rwr", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | | | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | + | --> | |
| - | + | {{STRUCTURE_1rwr| PDB=1rwr | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Crystal structure of filamentous hemagglutinin secretion domain''' | '''Crystal structure of filamentous hemagglutinin secretion domain''' | ||
| Line 27: | Line 24: | ||
[[Category: Clantin, B.]] | [[Category: Clantin, B.]] | ||
[[Category: Villeret, V.]] | [[Category: Villeret, V.]] | ||
| - | [[Category: | + | [[Category: Adhesin]] |
| - | [[Category: | + | [[Category: Beta-helix]] |
| - | [[Category: | + | [[Category: Filamentous hemagglutinin]] |
| - | [[Category: | + | [[Category: Tps domain]] |
| - | [[Category: | + | [[Category: Type v secretion]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:59:57 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 04:59, 3 May 2008
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 Page seeded by OCA on Sat May 3 07:59:57 2008
