Crystal structure of Escherichia coli CheY refined at 1.7-A resolution.
Crystal structure of Escherichia coli CheY refined at 1.7-A resolution.
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DOI：
10.2210/pdb3chy/pdb
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发表时间：
1993-01
期刊：
影响因子：
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通讯作者：
K. Volz;Philip Matsumura
中科院分区：
文献类型：
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作者：
K. Volz;Philip Matsumura
来自大肠杆菌的野生型CheY的三维结构已通过立体化学约束最小二乘最小化进行优化，在1.7 A分辨率下达到15.1%的晶体学R因子。该结构包含1165个原子，包括蛋白质的所有原子，147个水分子和3个硫酸根离子。最终模型的均方根偏差为0.018和0.049 A，从理想的键长和角距离，分别。七个氨基酸侧链已被建模的双重构象。CheY折叠成一个紧凑的（β/α）5球状蛋白，磷酸化区域包含在分子一面的空腔中。该活性位点区域由三条中心β链的羧基末端、α 1和连接β 5与α 5的环界定。该环的Lys-109侧链凭借其在Pro-110之前的顺式肽键构象延伸至活性位点。Lys-109的ε-氨基与Asp-57的羧基紧密结合，Asp-57是在CheY的活化过程中被磷酸化的残基。磷酸化区域中氢键网络的细节表明结构重排必须伴随着Asp-57的磷酸化。
The three-dimensional structure of wild-type CheY from Escherichia coli has been refined by stereochemically restrained least squares minimization to a crystallographic R-factor of 15.1% at 1.7-A resolution. The structure contains 1165 atoms, including all atoms of the protein, 147 water molecules, and three sulfate ions. The final model has root mean square deviations of 0.018 and 0.049 A from idealized bond lengths and angle distances, respectively. Seven amino acid side chains have been modeled in dual conformations. CheY folds as a compact (beta/alpha)5 globular protein, with the phosphorylation region contained in a cavity on one face of the molecule. This active site area is bordered by the carboxyl termini of the three central beta-strands, by alpha 1, and by the loop connecting beta 5 to alpha 5. The Lys-109 side chain of this loop extends into the active site by virtue of its cis peptide bond conformation preceding Pro-110. The epsilon-amino group of Lys-109 is in close bonding contact with the carboxyl group of Asp-57, the residue that is phosphorylated in the activation process of CheY. The details of the hydrogen bonding network in the phosphorylation region indicate that structural rearrangements must accompany the phosphorylation of Asp-57.