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1ry9
From Proteopedia
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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 CL 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
Page seeded by OCA on Wed Nov 21 01:57:11 2007
