6RN5

PptA from Streptomyces chartreusis

6RN5 の概要

• エントリーDOI: 10.2210/pdb6rn5/pdb
• 分子名称: CHAD domain protein, COPPER (II) ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: polyphosphate-binding protein, unknown function
• 由来する生物種: Streptomyces chartreusis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40290.98

構造登録者

Werten, S.,Rustmeier, N.H.,Hinrichs, W. (登録日: 2019-05-08, 公開日: 2019-06-19, 最終更新日: 2024-05-15)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.037 Å)