期刊
JOURNAL OF INORGANIC BIOCHEMISTRY
卷 223, 期 -, 页码 -出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2021.111554
关键词
Urease activation; Nickel transport; Protein tunnels; Enhanced sampling molecular dynamics; Path-collective variables; Helicobacter pylori
资金
- CINECA
- CIRMMP (Consorzio Interuniversitario di Risonanze Magnetiche di Metallo-Proteine)
The survival of pathogenic bacteria like Helicobacter pylori relies on the activity of nickel dependent enzyme urease. Nickel insertion into urease is mediated by a multimeric chaperone complex. Research suggests that nickel can be transported through a series of stations found along internal pathways.
The survival of several pathogenic bacteria, such as Helicobacter pylori (Hp), relies on the activity of the nickel dependent enzyme urease. Nickel insertion into urease is mediated by a multimeric chaperone complex (HpUreDFG) that is responsible for the transport of Ni(II) from a conserved metal binding motif located in the UreG dimer (CPH motif) to the catalytic site of the enzyme. The X-ray structure of HpUreDFG revealed the presence of water-filled tunnels that were proposed as a route for Ni(II) translocation. Here, we probe the transport of Ni(II) through the internal tunnels of HpUreDFG, from the CPH motif to the external surface of the complex, using microsecond-long enhanced molecular dynamics simulations. The results suggest a bucket brigade mechanism whereby Ni(II) can be transported through a series of stations found along these internal pathways.
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