8ara

Heterologous Complex of Aeromonas hydrophila Type III secretion substrate AscX with Yersinia enterocolitica chaperone YscY

spinqualitylabelsall models 8ara, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ara is a 4 chain structure with sequence from Aeromonas hydrophila and Yersinia enterocolitica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: ACT, CL, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q699R5_AERHY Publication Abstract from PubMed Gram-negative bacteria such as Aeromonas and Yersinia spp. have developed mechanisms to inhibit the immune defense of their host. Effector proteins are directly injected into the host cytoplasm from the bacterial cytosol via type III secretion systems (T3SSs), where they modulate the cytoskeleton and signaling of the cell. Assembly of, and secretion via, T3SSs is tightly regulated by a number of bacterial proteins, including SctX (AscX in Aeromonas), the secretion of which is essential for T3SS function. Here, crystal structures of AscX in complex with SctY chaperones from Yersinia or Photorhabdus spp. carrying homologous T3SSs are described. There are crystal pathologies in all cases, with one crystal form diffracting anisotropically and the other two exhibiting strong pseudotranslation. The new structures reveal that the positioning of the substrate is very similar on different chaperones. However, the two C-terminal SctX helices that cap the N-terminal tetratricopeptide repeat of SctY shift and tilt depending on the identity of the chaperone. Moreover, the C-terminus of the alpha3 helix of AscX exhibits an unprecedented kink in two of the structures. In previous structures, the C-terminus of SctX protrudes beyond the chaperone as a straight helix: a conformation that is required for binding to the nonameric export gate SctV but that is unfavorable for binary SctX-SctY complexes due to the hydrophobicity of helix alpha3 of SctX. A kink in helix alpha3 may allow the chaperone to shield the hydrophobic C-terminus of SctX in solution. The type III secretion chaperone SctY may shield the hydrophobic export gate-binding C-terminus of its substrate SctX.,Gilzer D, Kowal JL, Flottmann F, Niemann HH Acta Crystallogr D Struct Biol. 2023 Jun 1;79(Pt 6):508-517. doi: , 10.1107/S2059798323003248. Epub 2023 May 19. PMID:37204817 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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