3gyz

Crystal structure of IpgC from Shigella flexneri

spinqualitylabelsall models 3gyz, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3gyz 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 2.15Å Ligands: GOL, NA, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function IPGC_SHIFL Assists the correct folding of nascent IpaB. Once it is bound to IpaB, it binds to IpaC and impedes their premature association that would lead to their degradation in the absence of IpcG. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The delivery of virulence factors into host cells through type III secretion systems is essential for enterobacterial pathogenesis. Molecular chaperones bind specifically to virulence factors in the bacterial cytosol before secretion. Invasion plasmid gene C (IpgC) is a chaperone that binds 2 essential virulence factors of Shigella: invasion plasmid antigens (Ipa) B and C. Here, we report the crystal structure of IpgC alone and in complex with the chaperone binding domain (CBD) of IpaB. The chaperone captures the CBD in an extended conformation that is stabilized by conserved residues lining the cleft. Analysis of the cocrystal structure reveals a sequence motif that is functional in the IpaB translocator class from different bacteria as determined by isothermal titration calorimetry. Our results show how translocators are chaperoned and may allow the design of inhibitors of enterobacterial diseases. IpaB-IpgC interaction defines binding motif for type III secretion translocator.,Lunelli M, Lokareddy RK, Zychlinsky A, Kolbe M Proc Natl Acad Sci U S A. 2009 May 28. PMID:19478065 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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