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Title | Structural and biochemical analysis of a phosin from Streptomyces chartreusis reveals a combined polyphosphate- and metal-binding fold. |
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Journal, issue, pages | FEBS Lett, Vol. 593, Issue 15, Page 2019-2029, Year 2019 |
Publish date | Jun 17, 2019 |
![]() | Sebastiaan Werten / Nils Hinnerk Rustmeier / Maximilian Gemmer / Marie-Joëlle Virolle / Winfried Hinrichs / ![]() ![]() ![]() |
PubMed Abstract | 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 ...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. |
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Methods | SAS (X-ray synchrotron) / X-ray diffraction |
Resolution | 2.037 Å |
Structure data | ![]() SASDF76: ![]() PDB-6rn5: |
Chemicals | ![]() ChemComp-CU: ![]() ChemComp-CL: ![]() ChemComp-SO4: ![]() ChemComp-CO3: ![]() ChemComp-HOH: |
Source |
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![]() | UNKNOWN FUNCTION / Polyphosphate-binding protein |