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Structural and biochemical analysis of a phosin from Streptomyces chartreusis reveals a combined polyphosphate‐ and metal‐binding fold

X‐ray crystallographic analysis of a phosin (PptA) from Steptomyces chartreusis reveals a metal‐associated, lozenge‐shaped fold featuring a 5–10 Å wide, positively charged tunnel that traverses the protein core. Two distinct metal‐binding sites were identified in which the predominant metal ion was...

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Detalles Bibliográficos
Autores principales:	Werten, Sebastiaan, Rustmeier, Nils Hinnerk, Gemmer, Maximilian, Virolle, Marie‐Joëlle, Hinrichs, Winfried
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	John Wiley and Sons Inc. 2019
Materias:	Research Articles
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6771595/ https://www.ncbi.nlm.nih.gov/pubmed/31183865 http://dx.doi.org/10.1002/1873-3468.13476

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