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Structural and Biochemical Analysis of a Phosin from Streptomyces chartreusis Reveals a Combined Polyphosphate- and Metal-Binding Fold

Abstract : X-ray crystallographic analysis of a phosin (PptA) from Steptomyces chartreusis reveals a metal-associated, lozenge-shaped fold featuring a 5–10 angström wide, positively charged tunnel that traverses the protein core. Two distinct metal-binding sites were identified in which the predominant metal ion was Cu2+. In solution, PptA forms stable homodimers that bind with nanomolar affinity to polyphosphate, a stress-related biopolymer acting as a phosphate and energy reserve in conditions of nutrient depletion. A single protein dimer interacts with 14–15 consecutive phosphate moieties within the polymer. Our observations suggest that PptA plays a role in polyphosphate metabolism, mobilisation or sensing, possibly by acting in concert with polyphosphate kinase (Ppk). Like Ppk, phosins may influence antibiotic synthesis by streptomycetes.
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https://hal.archives-ouvertes.fr/hal-02174917
Contributor : Marie-Claude Serre <>
Submitted on : Wednesday, November 25, 2020 - 11:16:28 AM
Last modification on : Wednesday, November 25, 2020 - 11:23:13 AM

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Sebastiaan Werten, Nils Hinnerk Rustmeier, Maximilian Gemmer, Marie-Joëlle Virolle, Winfried Hinrichs. Structural and Biochemical Analysis of a Phosin from Streptomyces chartreusis Reveals a Combined Polyphosphate- and Metal-Binding Fold. FEBS Letters, Wiley, 2019, Epub ahead of print. ⟨10.1002/1873-3468.13476⟩. ⟨hal-02174917⟩

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