尿嘧啶-DNA糖基化酶抑制蛋白的三级结构。
Tertiary structure of uracil-DNA glycosylase inhibitor protein.
作者信息
Beger R D, Balasubramanian S, Bennett S E, Mosbaugh D W, Bolton P H
机构信息
Chemistry Department, Wesleyan University, Middletown, Connecticut 06459, USA.
出版信息
J Biol Chem. 1995 Jul 14;270(28):16840-7. doi: 10.1074/jbc.270.28.16840.
The Bacillus subtilis bacteriophage PBS2 uracil-DNA glycosylase inhibitor (Ugi) is an acidic protein of 84 amino acids that inactivates uracil-DNA glycosylase from diverse organisms. The secondary structure of Ugi consists of five anti-parallel beta-strands and two alpha-helices (Balasubramanian, S., Beger, R.D., Bennett, S.E., Mosbaugh, D.W., and Bolton, P.H. (1995) J. Biol. Chem. 270, 296-303). The tertiary structure of Ugi has been determined by solution state multidimensional nuclear magnetic resonance. The Ugi structure contains an area of highly negative electrostatic potential produced by the close proximity of a number of acidic residues. The unfavorable interactions between these acidic residues are apparently accommodated by the stability of the beta-strands. This negatively charged region is likely to play an important role in the binding of Ugi to uracil-DNA glycosylase.
枯草芽孢杆菌噬菌体PBS2尿嘧啶-DNA糖基化酶抑制剂（Ugi）是一种由84个氨基酸组成的酸性蛋白质，它能使来自不同生物体的尿嘧啶-DNA糖基化酶失活。Ugi的二级结构由五条反平行β链和两条α螺旋组成（巴拉苏布拉马尼亚姆，S.，贝格尔，R.D.，贝内特，S.E.，莫斯博，D.W.，和博尔顿，P.H.（1995年）《生物化学杂志》270，296 - 303）。Ugi的三级结构已通过溶液态多维核磁共振确定。Ugi结构包含一个由许多酸性残基紧密靠近产生的高度负静电势区域。这些酸性残基之间不利的相互作用显然通过β链的稳定性得到了调节。这个带负电荷的区域可能在Ugi与尿嘧啶-DNA糖基化酶的结合中起重要作用。
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