3ml3
From Proteopedia
Crystal structure of the IcsA autochaperone region
Structural highlights
Function[ICSA_SHIFL] Essential for bacterial spreading by eliciting polar deposition of filamentous actin (actin-based motility). Inside the host cell mediates nucleation and polymerization of actin molecules on the bacterial surface, which provides the propulsive force for intracellular movement and intercellular dissemination of the bacterium. During invasion of mammalian cells, triggers autophagy by binding to APG5L. Interaction with IcsB leads to escape from the autophagic host defense system. Also binds ATP and displays weak ATPase activity.[1] [2] [3] [4] [5] Publication Abstract from PubMedThe IcsA (intracellular spread gene A) autotransporter from Shigella flexneri is a key virulence factor. We identified a stable fragment comprising residues 591 to 758, which corresponds to the autochaperone region of the IcsA passenger domain. We showed that thermal unfolding of the autochaperone region is reversible and determined its crystal structure at 2.0-A resolution. Crystal Structure of the Autochaperone Region from the Shigella flexneri Autotransporter IcsA.,Kuhnel K, Diezmann D J Bacteriol. 2011 Apr;193(8):2042-5. Epub 2011 Feb 18. PMID:21335457[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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