| 引用本文: | 米晓钰,李乔,马睿,朱晓林,温永强,刘霞,杜晓华.天祝白牦牛与黄牛NGB蛋白三级结构比较分析[J].生物信息学,2021,19(1):55-65. |
| MI Xiaoyu,LI Qiao,MA Rui,ZHU Xiaolin,WEN Yongqiang,LIU Xia,DU Xiaohua2.Comparative analysis of three-dimensional structure of neuroglobin protein in Tianzhu white yak and cattle[J].Chinese Journal of Bioinformatics,2021,19(1):55-65. |
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| 天祝白牦牛与黄牛NGB蛋白三级结构比较分析 |
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米晓钰1,李乔1,马睿1,朱晓林1,温永强1,刘霞1,杜晓华2
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(1.甘肃农业大学 生命科学技术学院, 兰州 730070;2. 甘肃农业大学 动物医学院,兰州 730070)
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| 摘要: |
| 通过比较天祝白牦牛(Bos grunniens)与黄牛(Bos taurus)NGB蛋白三级结构,分析天祝白牦牛NGB蛋白氨基酸位点突变对其三级结构的影响。利用生物信息学在线分析网站及软件对天祝白牦牛和黄牛NGB蛋白的同源性、系统发育进化、三级结构进行比较分析。结果显示,天祝白牦牛NGB蛋白进化趋于保守,83号位点为未知突变,97号位点为保守替换；83号位点突变使得NGB蛋白Ser突变为Pro,主要为R侧链由醇羟基突变为四碳环,侧链结构发生改变,使得83号位点由α-螺旋突变为无规卷曲,突变位于E、F链之间,使得E、F链之间的距离由11.79 变为8.21 ,致使与卟啉环中心铁原子相连远端His 64 距离由2.17 变为2.10 ；97号位点突变使得NGB蛋白Arg突变为Gln,主要为R侧链由氮原子突变为氧原子,且与碳原子通过双键连接,侧链结构未发生改变,使得97号位点突变后仍为α-螺旋,突变基团指向亲水相,羧基端与近端His 96位点相连,致使His 96与卟啉环中心铁原子距离由1.98 变为2.00 。经比较天祝白牦牛两处突变未发生在NGB蛋白核心功能区,对NGB蛋白功能未产生影响；突变造成R侧链基团发生改变,可能对NGB蛋白稳定性、柔韧性及溶解度造成一定影响；核心His 64、His 96与卟啉环中心铁原子距离发生改变,说明突变极有可能会对血红素外源配体结合造成一定影响。 |
| 关键词: 天祝白牦牛 黄牛 NGB蛋白 三级结构 |
| DOI：10.12113/202004003 |
| 分类号:Q518.2 |
| 文献标识码:A |
| 基金项目:国家自然科学基金地区科学基金(No.31760305); 甘肃农业大学青年导师基金项目(No.GAU-QNDS- 201501); 甘肃省科技计划项目(No.17JR5RA142). |
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| Comparative analysis of three-dimensional structure of neuroglobin protein in Tianzhu white yak and cattle |
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MI Xiaoyu1, LI Qiao1, MA Rui1, ZHU Xiaolin1, WEN Yongqiang1, LIU Xia1, DU Xiaohua2
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(1.College of Life Science and Technology,Gansu Agricultural University, Lanzhou 730070, China; 2.College of Veterinary Medicine,Gansu Agricultural University, Lanzhou 730070, China)
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| Abstract: |
| The study compared the three-dimensional structures of neuroglobin (NGB) protein in Tianzhu white yak(Bos grunniens) and cattle(Bos taurus), and analyzed the effect of amino acid site mutation of NGB protein in Tianzhu white yak on its three-dimensional structure. The bioinformatics online analysis website and software were used to compare and analyze the homology, phylogenetic evolution, and three-dimensional structure of NGB protein in Tianzhu white yak and yellow cattle. Results showed that the evolution of Tianzhu white yak NGB protein tended to be conservative, where the 83rd site of Tianzhu white yak NGB protein was an unknown mutation and the 97rd site was a conservative substitution. Three-dimensional structure analysis revealed that the mutation of the 83rd site caused the mutation of the NGB protein Ser to Pro.The main reason was that the R side chain was mutated from alcohol hydroxy group to four carbon ring, and the overall side chain structure changed, so the 83rd site changed from α-helices to random coil. The mutation located between E and F chains, and the spacing between the E and F chains changed from 11.79 to 8.21 , resulting in the distance from the center of the porphyrin ring to the distal His 64 changed from 2.17 to 2.10 . The mutation of the 97th site caused the NGB protein Arg to be mutated to Gln. It was mainly because the R side chain was mutated from nitrogen atom to oxygen atom and was linked to the carbon atom through a double bond, and the overall side chain structure was not changed.Therefore,the 97th site after mutation remained to be α-helices, the mutated group pointed to the hydrophilic phase, and the carboxy terminus was linked to the proximal His 96 site, resulting in the distance between the His 96 and the porphyrin ring center changed from 1.98 to 2.00 . After comparison, the two mutations in Tianzhu white yak did not occur in the core functional region of NGB protein, which had no effect on the function of NGB protein. The mutations caused the change of R side chain group, which may have effects on the stability, flexibility, and solubility of NGB protein. The distance between core His 64, His 96, and porphyrin ring center changed, indicating that the mutation is likely to affect the heme exogenous ligand binding. |
| Key words: Tianzhu white yak Cattle NGB protein Three-dimensional structure |
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