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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...
| Autores principales: | , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
John Wiley and Sons Inc.
2019
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| Materias: | |
| 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 |