当前位置: X-MOL 学术Proteins Struct. Funct. Bioinform. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Crystal structure of PYCH_01220 from Pyrococcus yayanosii potentially involved in binding nucleic acid
Proteins: Structure, Function, and Bioinformatics ( IF 3.2 ) Pub Date : 2020-11-25 , DOI: 10.1002/prot.26029
Haemin Noh 1 , Jae-Hyun Jeon 1 , Yeon-Gil Kim 2 , Byung-Ha Oh 1
Affiliation  

We report the crystal structure of PYCH_01220, a hypothetical protein in Pyrococcus yayanosii CH1. This protein is composed of two domains, named Domain A and Domain B. While Domain B is not significantly homologous to known protein structures, Domain A is structurally analogous to the C‐terminal ribonuclease domain of Escherichia coli colicin D. Domain A has a positively charged surface patch rendered by 13 basic residues, eight arginine or lysine residues of which are evolutionarily conserved. Electrophoretic mobility shift assays showed that PYCH_01220 binds to DNA, and charge‐inversion mutations on this patch negatively affect the DNA binding, suggesting that the function of PYCH_01220 might involve nucleic acid‐binding via the positively charged patch.

中文翻译:

来自 Pyrococcus yayanosii 的 PYCH_01220 的晶体结构可能参与结合核酸

我们报告了 PYCH_01220 的晶体结构,PYCH_01220 是Pyrococcus yayanosii CH1 中的一种假设蛋白。该蛋白质由两个结构域组成,称为结构域 A 和结构域 B。虽然结构域 B 与已知的蛋白质结构没有显着同源性,但结构域 A 在结构上与大肠杆菌素 D的 C 端核糖核酸酶结构域相似。结构域 A 具有阳性由 13 个碱性残基呈现的带电表面补丁,其中 8 个精氨酸或赖氨酸残基在进化上是保守的。电泳迁移率变化分析表明 PYCH_01220 与 DNA 结合,并且该贴片上的电荷反转突变对 DNA 结合产生负面影响,表明 PYCH_01220 的功能可能涉及通过带正电的贴片与核酸结合。
更新日期:2020-11-25
down
wechat
bug