8HC1

CryoEM structure of Helicobacter pylori UreFD/urease complex

This is a non-PDB format compatible entry.

Summary for 8HC1

• Entry DOI: 10.2210/pdb8hc1/pdb
• EMDB information: 34648 34659
• Descriptor: Urease subunit alpha, Urease subunit beta, Urease accessory protein UreH, ... (4 entities in total)
• Functional Keywords: urease, activation complex, urea, ureb, urec, uref, ured, ureh, helicobacter pylori, hydrolase
• Biological source: Helicobacter pylori 26695; More
• Total number of polymer chains: 48
• Total formula weight: 1771272.59

Authors

Nim, Y.S.,Fong, I.Y.H.,Deme, J.,Tsang, K.L.,Caesar, J.,Johnson, S.,Wong, K.B.,Lea, S.M. (deposition date: 2022-11-01, release date: 2023-05-03, Last modification date: 2024-06-19)

Primary citation

Nim, Y.S.,Fong, I.Y.H.,Deme, J.,Tsang, K.L.,Caesar, J.,Johnson, S.,Pang, L.T.H.,Yuen, N.M.H.,Ng, T.L.C.,Choi, T.,Wong, Y.Y.H.,Lea, S.M.,Wong, K.B.
Delivering a toxic metal to the active site of urease.
Sci Adv, 9:eadf7790-eadf7790, 2023

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 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.

PubMed: 37083535
DOI: 10.1126/sciadv.adf7790

Experimental method

ELECTRON MICROSCOPY (2.3 Å)