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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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| Yayımlandı: | FEBS Lett |
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| Asıl Yazarlar: | , , , , |
| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
John Wiley and Sons Inc.
2019
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| Konular: | |
| Online Erişim: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6771595/ https://ncbi.nlm.nih.gov/pubmed/31183865 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/1873-3468.13476 |
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