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| '''Spa15, a Type III Secretion Chaperone from Shigella flexneri'''
| | ===Spa15, a Type III Secretion Chaperone from Shigella flexneri=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15088068}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15088068 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15088068}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Perez, J.]] | | [[Category: Perez, J.]] |
| [[Category: Alpha/beta fold]] | | [[Category: Alpha/beta fold]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:03:22 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:03:34 2008'' |
