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Structure of UreG/UreF/UreH Complex Reveals How Urease Accessory Proteins Facilitate Maturation of Helicobacter pylori Urease

DOI: 10.1371/journal.pbio.1001678 DOI Help
PMID: 24115911 PMID Help

Authors: Yu Hang Fong (University of Hong Kong) , Ho Chun Wong (University of Hong Kong) , Man Hon Yuen (University of Hong Kong) , Pak Ho Lau (University of Hong Kong) , Yu Wai Chen (King's College London) , Kam-bo Wong (University of Hong Kong) , Gregory A. Petsko (University of Hong Kong)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Plos Biology , VOL 11 (10)

State: Published (Approved)
Published: October 2013

Open Access Open Access

Abstract: Catalytic activities of many important enzymes depend upon metal cofactors. Ensuring each enzyme acquires the proper type of metal cofactor is essential to life. One such example is urease, which is a nickel containing metalloenzyme catalyzing the hydrolysis of urea to ammonia. The survival of Helicobacter pylori, a stomach ulcer–causing pathogen, in the human stomach depends on the ammonia released to neutralize gastric acid. In this study, we revealed the detail mechanism of how urease accessory proteins UreF, UreH, and UreG cooperate to couple GTP hydrolysis to deliver nickel to urease.

Journal Keywords: Crystallography ; X-Ray ; Guanosine; Helicobacter; Hydrolysis ; Ions ; Models ; Molecular ; Nickel ; Protein; Urease

Subject Areas: Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography