Structural highlights
Publication Abstract from PubMed
X-ray crystallographic analysis of a phosin (PptA) from Steptomyces chartreusis reveals a metal-associated, lozenge-shaped fold featuring a 5-10 A 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.
Structural and biochemical analysis of a phosin from Streptomyces chartreusis reveals a combined polyphosphate- and metal-binding fold.,Werten S, Rustmeier NH, Gemmer M, Virolle MJ, Hinrichs W FEBS Lett. 2019 Jun 10. doi: 10.1002/1873-3468.13476. PMID:31183865[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Werten S, Rustmeier NH, Gemmer M, Virolle MJ, Hinrichs W. Structural and biochemical analysis of a phosin from Streptomyces chartreusis reveals a combined polyphosphate- and metal-binding fold. FEBS Lett. 2019 Jun 10. doi: 10.1002/1873-3468.13476. PMID:31183865 doi:http://dx.doi.org/10.1002/1873-3468.13476
