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-Structure paper
Title | Delivering a toxic metal to the active site of urease. |
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Journal, issue, pages | Sci Adv, Vol. 9, Issue 16, Page eadf7790, Year 2023 |
Publish date | Apr 21, 2023 |
Authors | Yap Shing Nim / Ivan Yu Hang Fong / Justin Deme / Ka Lung Tsang / Joseph Caesar / Steven Johnson / Longson Tsz Hin Pang / Nicholas Man Hon Yuen / Tin Long Chris Ng / Tung Choi / Yakie Yat Hei Wong / Susan M Lea / Kam-Bo Wong / |
PubMed Abstract | Urease is a nickel (Ni) enzyme that is essential for the colonization of in the human stomach. To solve the problem of delivering the toxic Ni ion to the active site without diffusing into the ...Urease is a nickel (Ni) enzyme that is essential for the colonization of 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 UreFD/urease and 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. |
External links | Sci Adv / PubMed:37083535 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.3 - 2.7 Å |
Structure data | EMDB-34648, PDB-8hc1: EMDB-34659, PDB-8hcn: |
Source |
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Keywords | HYDROLASE / Urease / activation complex / UreA / UreB / UreC / UreF / UreD / UreH / Helicobacter pylori / Klebsiella pneumoniae |