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| - | [[Image:1rwr.gif|left|200px]] | + | {{Seed}} |
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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'''
| + | ===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 >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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15079085}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15079085 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15079085}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Tps domain]] | | [[Category: Tps domain]] |
| | [[Category: Type v secretion]] | | [[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 Tue Jul 29 11:36:55 2008'' |
Revision as of 08:36, 29 July 2008
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
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