5ke1

Structure of a C-terminal fragment of the IcsA/VirG passenger-domain

spinqualitylabelsall models 5ke1, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ke1 is a 2 chain structure with sequence from Shigella flexneri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: NI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. Publication Abstract from PubMed IcsA/VirG is a key virulence factor of the human pathogen Shigella flexneri, acting as both an adhesin and actin-polymerizing factor during infection. We identified a soluble expression construct of the IcsA/VirG alpha-domain using the ESPRIT library screening system and determined its structure to 1.9A resolution. In addition to the previously characterized autochaperone domain, our structure reveals a new domain, which shares a common fold with the autochaperone domains of various autotransporters. We further provide insight into the previously structurally uncharacterized beta-helix domain that harbors the polar targeting motif and passenger-associated transport repeat. This structure is the first of any member of the recently identified passenger-associated transport repeat-containing autotransporters. Thus, it provides new insights into the overall architecture of this class of autotransporters, the function of the identified additional autochaperone domain and the structural properties of motifs involved in polar targeting and secretion of the Shigella flexneri virulence factor IcsA/VirG. Structural insights into the architecture of the Shigella flexneri virulence factor IcsA/VirG and motifs involved in polar distribution and secretion.,Leupold S, Busing P, Mas PJ, Hart DJ, Scrima A J Struct Biol. 2017 Mar 6. pii: S1047-8477(17)30037-0. doi:, 10.1016/j.jsb.2017.03.003. PMID:28268178 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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