Phosphate uptake in PhoX: Molecular mechanisms.
Int J Biol Macromol
; 269(Pt 1): 131993, 2024 Jun.
Article
em En
| MEDLINE
| ID: mdl-38705335
ABSTRACT
PhoX is a high-affinity phosphate binding protein, present in Xanthomonas citri, a phytopathogen responsible for the citrus canker disease. Performing molecular dynamics simulations and different types of computational analyses, we study the molecular mechanisms at play in relation to phosphate binding, revealing the global functioning of the protein PhoX naturally oscillates along its global normal modes, which allow it to explore both bound and unbound conformations, eventually attracting a nearby negative phosphate ion to the highly positive electrostatic potential on its surface, particularly close to the binding pocket. There, several hydrogen bonds are formed with the two main domains of the structure. Phosphate creates, in this way, a strong bridge that connects the domains, keeping itself between them, in a tight closed conformation, explaining its high binding affinity.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Fosfatos
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Proteínas de Bactérias
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Xanthomonas
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Simulação de Dinâmica Molecular
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article