1ry9
From Proteopedia
(New page: 200px<br /><applet load="1ry9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ry9, resolution 1.82Å" /> '''Spa15, a Type III Se...) |
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| - | [[Image:1ry9.jpg|left|200px]]<br /><applet load="1ry9" size=" | + | [[Image:1ry9.jpg|left|200px]]<br /><applet load="1ry9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ry9, resolution 1.82Å" /> | caption="1ry9, resolution 1.82Å" /> | ||
'''Spa15, a Type III Secretion Chaperone from Shigella flexneri'''<br /> | '''Spa15, a Type III Secretion Chaperone from Shigella flexneri'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Type III secretion (TTS) systems are used by many Gram-negative pathogens | + | Type III secretion (TTS) systems are used by many Gram-negative pathogens to inject virulence proteins into the cells of their hosts. Several of these virulence effectors require TTS chaperones that maintain them in a secretion-competent state. Whereas most chaperones bind only one effector, Spa15 from the human pathogen Shigella flexneri and homologous chaperones bind several seemingly unrelated effectors, and were proposed to form a special subgroup. Its 1.8 A crystal structure confirms this specific classification, showing that Spa15 has the same fold as other TTS effector chaperones, but forms a different dimer. The presence of hydrophobic sites on the Spa15 surface suggests that the different Spa15 effectors all possess similar structural elements that can bind these sites. Furthermore, the Spa15 structure reveals larger structural differences between class I chaperones than previously anticipated, which does not support the hypothesis that chaperone-effector complexes are structurally conserved and function as three-dimensional secretion signals. |
==About this Structure== | ==About this Structure== | ||
| - | 1RY9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1RY9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RY9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Shigella flexneri]] | [[Category: Shigella flexneri]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dijkstra, B | + | [[Category: Dijkstra, B W.]] |
| - | [[Category: Eerde, A | + | [[Category: Eerde, A van.]] |
[[Category: Hamiaux, C.]] | [[Category: Hamiaux, C.]] | ||
[[Category: Parsot, C.]] | [[Category: Parsot, C.]] | ||
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[[Category: alpha/beta fold]] | [[Category: alpha/beta fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:49 2008'' |
Revision as of 12:55, 21 February 2008
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Spa15, a Type III Secretion Chaperone from Shigella flexneri
Overview
Type III secretion (TTS) systems are used by many Gram-negative pathogens to inject virulence proteins into the cells of their hosts. Several of these virulence effectors require TTS chaperones that maintain them in a secretion-competent state. Whereas most chaperones bind only one effector, Spa15 from the human pathogen Shigella flexneri and homologous chaperones bind several seemingly unrelated effectors, and were proposed to form a special subgroup. Its 1.8 A crystal structure confirms this specific classification, showing that Spa15 has the same fold as other TTS effector chaperones, but forms a different dimer. The presence of hydrophobic sites on the Spa15 surface suggests that the different Spa15 effectors all possess similar structural elements that can bind these sites. Furthermore, the Spa15 structure reveals larger structural differences between class I chaperones than previously anticipated, which does not support the hypothesis that chaperone-effector complexes are structurally conserved and function as three-dimensional secretion signals.
About this Structure
1RY9 is a Single protein structure of sequence from Shigella flexneri with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specificity., van Eerde A, Hamiaux C, Perez J, Parsot C, Dijkstra BW, EMBO Rep. 2004 May;5(5):477-83. Epub 2004 Apr 16. PMID:15088068
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