8dol

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

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== 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<ref>PMID:36717564</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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