Probing the transport of Ni(II) ions through the internal tunnels of the Helicobacter pylori UreDFG multimeric protein complex.
J Inorg Biochem
; 223: 111554, 2021 10.
Article
em En
| MEDLINE
| ID: mdl-34325209
ABSTRACT
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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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
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Helicobacter pylori
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Chaperonas Moleculares
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Níquel
Idioma:
En
Ano de publicação:
2021
Tipo de documento:
Article