(1)H, (13)C, (15)N backbone and side chain NMR resonance assignments for E73 from Sulfolobus spindle-shaped virus ragged hills, a hyperthermophilic crenarchaeal virus from Yellowstone National Park.

(1)H, (13)C, (15)N backbone and side chain NMR resonance assignments for E73 from Sulfolobus spindle-shaped virus ragged hills, a hyperthermophilic crenarchaeal virus from Yellowstone National Park.
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DOI:
10.1007/s12104-009-9179-z
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发表时间:
2009-12
影响因子:
0.9
通讯作者:
Copié V
Copié V
中科院分区:
生物学4区
文献类型:
--
作者:
Schlenker C;Menon S;Lawrence CM;Copié V

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泉古菌病毒通常在高温酸性环境中发现,如黄石国家公园。这些引人注目的病毒不仅表现出不寻常的形态,而且还表现出极端的遗传多样性。然而,很少有人知道crenarchaeal病毒的生命周期,病毒与宿主的相互作用,以及他们的适应极端嗜热环境。为了更好地了解泉古菌病毒的功能及其基因组编码的蛋白质,我们对硫化叶菌梭形病毒参差不齐的小山的开放阅读框架中编码的基因产物进行了详细的结构和功能研究。在此,我们报告(15 N,13 C,1H)共振分配的骨架和侧链原子的19.1 kDa的同源二聚体E73蛋白的SSVRH。
Crenarchaeal viruses are commonly found in hyperthermal acidic environments such as those of Yellow-stone National Park. These remarkable viruses not only exhibit unusual morphologies, but also display extreme genetic diversity. However, little is known about crenarchaeal viral life cycles, virus–host interactions, and their adaptation to hyperthermophilic environments. In an effort to better understand the functions of crenarchaeal viruses and the proteins encoded by their genomes, we have undertaken detailed structural and functional studies of gene products encoded in the open reading frames of Sulfolobus spindle-shaped virus ragged hills. Herein, we report (15N, 13C, 1H) resonance assignments of backbone and side chain atoms of a 19.1 kDa homodimeric E73 protein of SSVRH.
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