Solution structure of the M13 major coat protein in detergent micelles: a basis for a model of phage assembly involving specific residues.
Solution structure of the M13 major coat protein in detergent micelles: a basis for a model of phage assembly involving specific residues.
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洗涤剂胶束中 M13 主要外壳蛋白的溶液结构：涉及特定残基的噬菌体组装模型的基础。
DOI：
10.1006/jmbi.1998.1860
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发表时间：
1998
影响因子：
5.6
通讯作者：
C. W. Hilbers
中科院分区：
文献类型：
--
作者：
C. Papavoine;Boukje E. C. Christiaans;R. Folmer;Ruud N. H. Konings;C. W. Hilbers
利用异核多维核磁共振和约束分子动力学方法测定了溶解于洗涤剂胶束中的噬菌体M13的主要外壳蛋白的三维结构。该蛋白由两个α -螺旋组成，分别从残基8到16和25到45。这两个螺旋由一个柔性和扭曲的螺旋铰链区域连接。外壳蛋白的结构特性使它像一个连枷，其中疏水螺旋（残基25到45）是手柄，另一个两亲螺旋是摆动。在这个比喻中，铰链区域是连接皮革的一块。铰链区残基的可移动性很可能使其从膜结合形式（由洗涤剂胶束结构模拟）顺利转化为成熟噬菌体的结构。在主要外壳蛋白的膜结合形式的高分辨率结构以及成熟噬菌体的结构中，观察到两个螺旋表面上残基的特定分布。所有数据表明，这种残基排列对于蛋白质与膜的相互作用、噬菌体中正确的蛋白质- dna和蛋白质-蛋白质相互作用以及噬菌体在组装过程中的正常生长都是重要的。通过将我们的发现与洗涤剂胶束中主要外壳蛋白的早期NMR结果相结合，我们能够构建一个模型，解决特定残基在组装过程中的作用。
The three-dimensional structure of the major coat protein of bacteriophage M13, solubilized in detergent micelles, has been determined using heteronuclear multidimensional NMR and restrained molecular dynamics. The protein consists of two alpha-helices, running from residues 8 to 16 and 25 to 45, respectively. These two helices are connected by a flexible and distorted helical hinge region. The structural properties of the coat protein make it resemble a flail, in which the hydrophobic helix (residues 25 to 45) is the handle and the other, amphipathic, helix the swingle. In this metaphor, the hinge region is the connecting piece of leather. The mobility of the residues in the hinge region is likely to enable a smooth transformation from the membrane-bound form, mimicked by the structure in detergent micelles, into the structure in the mature phage. A specific distribution of the residues over the surface of the two helices was observed in the presented high-resolution structure of the membrane-bound form of the major coat protein as well as in the structure in the mature phage. All data suggest that this arrangement of residues is important for the interactions of the protein with the membrane, for correct protein-DNA and protein-protein interactions in the phage and for a proper growth of the phage during the assembly process. By combining our findings with earlier NMR results on the major coat protein in detergent micelles, we were able to construct a model that addresses the role of specific residues in the assembly process.
影响因子：
5.6
作者：
Overman, SA;Tsuboi, M;Thomas, GJ
通讯作者：
Thomas, GJ
膜结合噬菌体 Pf1 外壳蛋白的结构和动力学的 NMR 研究。
DOI：
10.1126/science.1925542
发表时间：
1991
期刊：
Science (New York, N.Y.)
影响因子：
--
作者：
Shon,KJ;Kim,Y;Colnago,LA;Opella,SJ
通讯作者：
Opella,SJ
DOI：
10.1093/protein/5.3.213
发表时间：
1992-04-01
期刊：
PROTEIN ENGINEERING
影响因子：
--
作者：
SCHIFFER, M;CHANG, CH;STEVENS, FJ
通讯作者：
STEVENS, FJ