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The structure of a tautomerase superfamily member linked to the type VI secretion system of Acinetobacter baumannii

Bacteria exploit specialized secretion systems to assist in competition for resources, in collaboration and in communication. Here, a protocol for the recombinant production, purification and crystallization of a protein linked to the Acinetobacter baumannii type VI secretion system is provided. A h...

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Detalles Bibliográficos
Autores principales: Pankov, Genady, Mol Avelar, Gabriela, Buchanan, Grant, Coulthurst, Sarah J., Hunter, William N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9813972/
https://www.ncbi.nlm.nih.gov/pubmed/36598351
http://dx.doi.org/10.1107/S2053230X22011414
Descripción
Sumario:Bacteria exploit specialized secretion systems to assist in competition for resources, in collaboration and in communication. Here, a protocol for the recombinant production, purification and crystallization of a protein linked to the Acinetobacter baumannii type VI secretion system is provided. A high-resolution structure of this trimeric protein is reported, revealing the characteristic dual β–α–β subunit fold typical of longer subunit members of the tautomerase superfamily. The protein does not appear to be toxic to bacteria or yeast under the conditions tested. The possible biological role of this protein is discussed.