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TitleStructural and biochemical analysis of a phosin from Streptomyces chartreusis reveals a combined polyphosphate- and metal-binding fold.
Journal, issue, pagesFEBS Lett, Vol. 593, Issue 15, Page 2019-2029, Year 2019
Publish dateJun 17, 2019
AuthorsSebastiaan Werten / Nils Hinnerk Rustmeier / Maximilian Gemmer / Marie-Joëlle Virolle / Winfried Hinrichs /
PubMed AbstractX-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 ...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 Cu . 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.
External linksFEBS Lett / PubMed:31183865 / PubMed Central
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution2.037 Å
Structure data

SASDF76:
Polyphosphate-targeting protein A (PptA)
Method: SAXS/SANS

PDB-6rn5:
PptA from Streptomyces chartreusis
Method: X-RAY DIFFRACTION / Resolution: 2.037 Å

Chemicals

ChemComp-CU:
COPPER (II) ION

ChemComp-CL:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-CO3:
CARBONATE ION

ChemComp-HOH:
WATER

Source
  • streptomyces chartreusis (bacteria)
KeywordsUNKNOWN FUNCTION / Polyphosphate-binding protein

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