Structural and biochemical analysis of a phosin from Streptomyces chartreusis reveals a combined polyphosphate‐ and metal‐binding fold
Structural and biochemical analysis of a phosin from Streptomyces chartreusis reveals a combined polyphosphate‐ and metal‐binding fold
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对来自 Chartreusis 链霉菌的磷苷进行结构和生化分析，揭示了多磷酸盐和金属结合折叠的组合
DOI：
10.1002/1873-3468.13476
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发表时间：
2019
期刊：
影响因子：
3.5
通讯作者：
W. Hinrichs
中科院分区：
文献类型：
--
作者：
S. Werten;N. Rustmeier;Maximilian Gemmer;M. Virolle;W. Hinrichs
X射线晶体学分析显示，来自黄绿色步霉菌的phosin （PptA）具有金属相关的菱形褶皱，具有5-10 Å宽的正电荷隧道穿过蛋白质核心。确定了两个不同的金属结合位点，其中主要的金属离子是Cu2+。在溶液中，PptA形成稳定的同型二聚体，与多磷酸盐结合，具有纳米摩尔亲和力，多磷酸盐是一种与应激相关的生物聚合物，在营养耗尽的条件下充当磷酸盐和能量储备。单个蛋白质二聚体与聚合物中14-15个连续的磷酸基团相互作用。我们的观察表明，PptA在多磷酸代谢、动员或传感中发挥作用，可能与多磷酸激酶（Ppk）协同作用。像Ppk一样，phosin可能影响链霉菌的抗生素合成。
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 Cu2+. 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.
影响因子：
3.9
作者：
Zheng, Heping;Chruszcz, Maksymilian;Minor, Wladek
通讯作者：
Minor, Wladek
影响因子：
4.4
作者：
Tumlirsch, Tony;Jendrossek, Dieter
通讯作者：
Jendrossek, Dieter