1rwr
From Proteopedia
(New page: 200px<br /><applet load="1rwr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rwr, resolution 1.72Å" /> '''Crystal structure of...) |
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| - | [[Image:1rwr.gif|left|200px]]<br /><applet load="1rwr" size=" | + | [[Image:1rwr.gif|left|200px]]<br /><applet load="1rwr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rwr, resolution 1.72Å" /> | caption="1rwr, resolution 1.72Å" /> | ||
'''Crystal structure of filamentous hemagglutinin secretion domain'''<br /> | '''Crystal structure of filamentous hemagglutinin secretion domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Filamentous hemagglutinin (FHA), the major 230-kDa adhesin of the whooping | + | 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== | ==About this Structure== | ||
| - | 1RWR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis]. Full crystallographic information is available from [http:// | + | 1RWR is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: type v secretion]] | [[Category: type v secretion]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:19 2008'' |
Revision as of 12:55, 21 February 2008
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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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