三维解决方案结构的n端接收器NTRC领域。
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Volkman BF, Nohaile MJ,艾米NK, Kustu年代,电话
三维解决方案结构的n端接收器NTRC领域。
生物化学。1995年1月31日,34 (4):1413 - 24。
- PubMed ID
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7827089 (在PubMed]
- 文摘
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NTRC转录增强子结合蛋白的n端结构域是一个家庭成员接收域的双组分调节系统。使用3 d和4 d NMR光谱,我们已经完成了1 h, 15 n, 13 c分配和确定解决方案结构的n端接收域的NTRC蛋白质。三维结构的测定进行了项目X-PLOR(共舞,1992)使用915 NMR-derived距离和二面角限制。合成的家庭结构平均均方根偏差的0.81的平均结构骨架原子参与定义良好的二级结构。的结构是由五个阿尔法螺旋和一个five-stranded平行β褶板,(β/α)5拓扑。比较解决方案的NTRC接收机的结构域与晶体结构的同源蛋白质崔氏在无镁(2 +)和镁(2 +)绑定形式(股票,点Mottonen, j . M。,股票,j·B。& shutt, c, e .自然(1989)337年,745 - 749;中场,K。& Matsumura p(1991)生物。化学。296年,15511 - 15519; Stock, A. M., Martinez-Hackert, E., Rasmussen, B. F., West, A. H., Stock, J. B., Ringe, D., & Petsko, G. A. (1993) Biochemistry 32, 13375-13380; Bellsolell, L., Prieto, J., Serrano, L., & Coll, M. (1994) J. Mol. Biol. 238, 489-495] reveals a very similar fold, with the only significant difference occurring in the positioning of helix 4 relative to the rest of the protein. Examination of the conformation of consensus residues of the receiver domain superfamily [Volz, K. (1993) Biochemistry 32, 11741-11753] in the structures of the NTRC receiver domain and CheY establishes the structural importance of residues whose side chains are involved in hydrogen bonding or hydrophobic core interactions. The importance of some nonconsensus residues which may be conserved for their ability to fulfill helix capping roles is also discussed.