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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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Shranjeno v:
Bibliografske podrobnosti
izdano v:FEBS Lett
Main Authors: Werten, Sebastiaan, Rustmeier, Nils Hinnerk, Gemmer, Maximilian, Virolle, Marie‐Joëlle, Hinrichs, Winfried
Format: Artigo
Jezik:Inglês
Izdano: John Wiley and Sons Inc. 2019
Teme:
Online dostop: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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