3w30

Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI

spinqualitylabelsall models 3w30, resolution 2.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3w30 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 2.99Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8VSD5_SHIFL Publication Abstract from PubMed Ubc13 is a ubiquitin-conjugating enzyme that plays a key role in the nuclear factor-kappaB signal transduction pathway in human diseases. The Shigella flexneri effector OspI affects inflammatory responses by catalyzing the deamidation of a specific glutamine residue at position 100 in Ubc13 during infection. This modification prevents the activation of the TNF (tumor necrosis factor) receptor-associated factor 6, leading to modulation of the diacylglycerol-CBM (CARD-Bcl10-Malt1) complex-TNF receptor-associated factor 6-nuclear factor-kappaB signaling pathway. To elucidate the structural basis of OspI function, we determined the crystal structures of the catalytically inert OspI C62A mutant and its complex with Ubc13 at resolutions of 3.0 and 2.96A, respectively. The structure of the OspI-Ubc13 complex revealed that the interacting surfaces between OspI and Ubc13 are a hydrophobic surface and a complementary charged surface. Furthermore, we predict that the complementary charged surface of OspI plays a key role in substrate specificity determination. Structural Basis for the Recognition of Ubc13 by the Shigella flexneri Effector OspI.,Nishide A, Kim M, Takagi K, Himeno A, Sanada T, Sasakawa C, Mizushima T J Mol Biol. 2013 Aug 9;425(15):2623-31. doi: 10.1016/j.jmb.2013.02.037. Epub 2013, Mar 27. PMID:23542009 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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