8hc1 | pdb_00008hc1

CryoEM structure of Helicobacter pylori UreFD/urease complex

spinqualitylabelsall models 8hc1, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8hc1 is a 48 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. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function URE23_HELPY Ammonia produced by ureolysis increases the gastric pH thereby providing an environment permissive for colonization of the stomach. Publication Abstract from PubMed Urease is a nickel (Ni) enzyme that is essential for the colonization of Helicobacter pylori in the human stomach. To solve the problem of delivering the toxic Ni ion to the active site without diffusing into the cytoplasm, cells have evolved metal carrier proteins, or metallochaperones, to deliver the toxic ions to specific protein complexes. Ni delivery requires urease to form an activation complex with the urease accessory proteins UreFD and UreG. Here, we determined the cryo-electron microscopy structures of H. pylori UreFD/urease and Klebsiella pneumoniae UreD/urease complexes at 2.3- and 2.7-angstrom resolutions, respectively. Combining structural, mutagenesis, and biochemical studies, we show that the formation of the activation complex opens a 100-angstrom-long tunnel, where the Ni ion is delivered through UreFD to the active site of urease. Delivering a toxic metal to the active site of urease.,Nim YS, Fong IYH, Deme J, Tsang KL, Caesar J, Johnson S, Pang LTH, Yuen NMH, Ng TLC, Choi T, Wong YYH, Lea SM, Wong KB Sci Adv. 2023 Apr 21;9(16):eadf7790. doi: 10.1126/sciadv.adf7790. Epub 2023 Apr , 21. PMID:37083535 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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