6rn5

PptA from Streptomyces chartreusis

spinqualitylabelsall models 6rn5, resolution 2.04Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6rn5 is a 1 chain structure with sequence from "actinomyces_chartreusis"_(leach_et_al._1953)_preobrazhenskaya_1966 "actinomyces chartreusis" (leach et al. 1953) preobrazhenskaya 1966. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, CO3, CU, SO4 Gene: SCNRRL3882_4295 ("Actinomyces chartreusis" (Leach et al. 1953) Preobrazhenskaya 1966) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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