Download MendeleyStructural and biochemical analysis of a phosin from Streptomyces chartreusis reveals a combined polyphosphate- and metal-binding fold.
Werten, S., Rustmeier, N.H., Gemmer, M., Virolle, M.J., Hinrichs, W.(2019) FEBS Lett 593: 2019-2029
- PubMed: 31183865
- DOI: https://doi.org/10.1002/1873-3468.13476
- Primary Citation of Related Structures:
6RN5 - 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 protein core. Two distinct metal-binding sites were identified in which the predominant metal ion was Cu 2+ . 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.
Organizational Affiliation:
Division of Biological Chemistry, Biocenter, Medical University of Innsbruck, Austria.
