1rwr
From Proteopedia
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| - | [[Image:1rwr.gif|left|200px]] | + | [[Image:1rwr.gif|left|200px]] |
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| - | '''Crystal structure of filamentous hemagglutinin secretion domain''' | + | {{Structure |
| + | |PDB= 1rwr |SIZE=350|CAPTION= <scene name='initialview01'>1rwr</scene>, resolution 1.72Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal structure of filamentous hemagglutinin secretion domain''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RWR is a [ | + | 1RWR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RWR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15079085 15079085] |
[[Category: Bordetella pertussis]] | [[Category: Bordetella pertussis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Clantin, B.]] | [[Category: Clantin, B.]] | ||
[[Category: Villeret, V.]] | [[Category: Villeret, V.]] | ||
| - | [[Category: | + | [[Category: adhesin]] |
[[Category: beta-helix]] | [[Category: beta-helix]] | ||
[[Category: filamentous hemagglutinin]] | [[Category: filamentous hemagglutinin]] | ||
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[[Category: type v secretion]] | [[Category: type v secretion]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:57:16 2008'' |
Revision as of 11:57, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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