8dol | pdb_00008dol

Mechanism of regulation of the Helicobacter pylori Cagbeta ATPase by CagZ

spinqualitylabelsall models 8dol, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8dol is a 6 chain structure with sequence from Helicobacter pylori 26695. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PEG, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O25260_HELPY Publication Abstract from PubMed The transport of the CagA effector into gastric epithelial cells by the Cag Type IV secretion system (Cag T4SS) of Helicobacter pylori (H. pylori) is critical for pathogenesis. CagA is recruited to Cag T4SS by the Cagbeta ATPase. CagZ, a unique protein in H. pylori, regulates Cagbeta-mediated CagA transport, but the underlying mechanisms remain unclear. Here we report the crystal structure of the cytosolic region of Cagbeta, showing a typical ring-like hexameric assembly. The central channel of the ring is narrow, suggesting that CagA must unfold for transport through the channel. Our structure of CagZ in complex with the all-alpha domain (AAD) of Cagbeta shows that CagZ adopts an overall U-shape and tightly embraces Cagbeta. This binding mode of CagZ is incompatible with the formation of the Cagbeta hexamer essential for the ATPase activity. CagZ therefore inhibits Cagbeta by trapping it in the monomeric state. Based on these findings, we propose a refined model for the transport of CagA by Cagbeta. Mechanism of regulation of the Helicobacter pylori Cagbeta ATPase by CagZ.,Wu X, Zhao Y, Zhang H, Yang W, Yang J, Sun L, Jiang M, Wang Q, Wang Q, Ye X, Zhang X, Wu Y Nat Commun. 2023 Jan 30;14(1):479. doi: 10.1038/s41467-023-36218-4. PMID:36717564 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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