6RN5

PptA from Streptomyces chartreusis

Summary for 6RN5

• Entry DOI: 10.2210/pdb6rn5/pdb
• Descriptor: CHAD domain protein, COPPER (II) ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: polyphosphate-binding protein, unknown function
• Biological source: Streptomyces chartreusis
• Total number of polymer chains: 1
• Total formula weight: 40290.98

Authors

Werten, S.,Rustmeier, N.H.,Hinrichs, W. (deposition date: 2019-05-08, release date: 2019-06-19, Last modification date: 2024-05-15)

Primary citation

Werten, S.,Rustmeier, N.H.,Gemmer, M.,Virolle, M.J.,Hinrichs, W.
Structural and biochemical analysis of a phosin from Streptomyces chartreusis reveals a combined polyphosphate- and metal-binding fold.
Febs Lett., 593:2019-2029, 2019

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 . 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.

PubMed: 31183865
DOI: 10.1002/1873-3468.13476

Experimental method

X-RAY DIFFRACTION (2.037 Å)