Structure of diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phospho­ribosylamino)uracil reductase from Acinetobacter baumannii

The bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-­amino-6-(5-phosphoribosylamino)uracil reductase (RibD) represents a potential antibacterial drug target. The structure of recombinant Acinetobacter baumannii RibD is reported in orthorhombic and tetragonal crystal forms at 2.2...

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Detalles Bibliográficos
Autores principales: Dawson, Alice, Trumper, Paul, Chrysostomou, Georgios, Hunter, William N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2013
Materias:
Structural Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3668577/
https://www.ncbi.nlm.nih.gov/pubmed/23722836
http://dx.doi.org/10.1107/S174430911301292X
Descripción
Sumario:The bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-­amino-6-(5-phosphoribosylamino)uracil reductase (RibD) represents a potential antibacterial drug target. The structure of recombinant Acinetobacter baumannii RibD is reported in orthorhombic and tetragonal crystal forms at 2.2 and 2.0 Å resolution, respectively. Comparisons with orthologous structures in the Protein Data Bank indicated close similarities. The tetragonal crystal form was obtained in the presence of guanosine monophosphate, which surprisingly was observed to occupy the adenine-binding site of the reductase domain.

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