Crystallization and preliminary crystallographic studies of PotA, a membrane-associated ATPase of the spermidine-preferential uptake system in Thermotoga maritime.
Crystallization and preliminary crystallographic studies of PotA, a membrane-associated ATPase of the spermidine-preferential uptake system in Thermotoga maritime.
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PotA 的结晶和初步晶体学研究，PotA 是海洋栖热袍菌亚精胺优先吸收系统的膜相关 ATP 酶。
DOI：
10.1107/s2053230x14008607
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发表时间：
2014
期刊：
影响因子：
--
通讯作者：
S. et al.
中科院分区：
文献类型：
--
作者：
Sugiyama;S. et al.
膜相关atp酶PotA是原核生物亚精胺优先摄取系统的一个组成部分，通过调节细胞多胺浓度在正常细胞生长中起重要作用。迄今为止，尚未确定多胺摄取系统中膜相关atp酶的三维结构。本文报道了海苔热藻中PotA的结晶和初步的x射线衍射分析。收集了原生和硒代蛋氨酸标记晶体的衍射数据，并将其处理到2.7 Å分辨率。初步的晶体分析表明，晶体属于六方空间群P3112（或P3212），其单位胞参数a = b = 88.9, c = 221.2 Å， α = 90, β = 90, γ = 120°，表明在不对称单元中存在二聚体。
A membrane-associated ATPase, PotA, is a component of the spermidine-preferential uptake system in prokaryotes that plays an important role in normal cell growth by regulating the cellular polyamine concentration. No three-dimensional structures of membrane-associated ATPases in polyamine-uptake systems have been determined to date. Here, the crystallization and preliminary X-ray diffraction analysis of PotA from Thermotoga maritima are reported. Diffraction data were collected and processed to 2.7 Å resolution from both native and selenomethionine-labelled crystals. Preliminary crystallographic analysis revealed that the crystals belonged to the hexagonal space group P3112 (or P3212), with unit-cell parameters a = b = 88.9, c = 221.2 Å, α = 90, β = 90, γ = 120°, indicating that a dimer was present in the asymmetric unit.