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1rwr

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[[Image:1rwr.gif|left|200px]]
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{{STRUCTURE_1rwr| PDB=1rwr | SCENE= }}
{{STRUCTURE_1rwr| PDB=1rwr | SCENE= }}
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'''Crystal structure of filamentous hemagglutinin secretion domain'''
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===Crystal structure of filamentous hemagglutinin secretion domain===
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==Overview==
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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 &gt;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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15079085 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15079085}}
==About this Structure==
==About this Structure==
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[[Category: Tps domain]]
[[Category: Tps domain]]
[[Category: Type v secretion]]
[[Category: Type v secretion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:59:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:36:55 2008''

Revision as of 08:36, 29 July 2008

Image:1rwr.png

Template:STRUCTURE 1rwr

Crystal structure of filamentous hemagglutinin secretion domain

Template:ABSTRACT PUBMED 15079085

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 Tue Jul 29 11:36:55 2008

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