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本文引用的文献

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Rewiring the specificity of two-component signal transduction systems.重新连接双组分信号转导系统的特异性。
Cell. 2008 Jun 13;133(6):1043-54. doi: 10.1016/j.cell.2008.04.040.
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Features of protein-protein interactions in two-component signaling deduced from genomic libraries.从基因组文库推导的双组分信号传导中蛋白质-蛋白质相互作用的特征
Methods Enzymol. 2007;422:75-101. doi: 10.1016/S0076-6879(06)22004-4.
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Functional dynamics of response regulators using NMR relaxation techniques.使用核磁共振弛豫技术研究响应调节蛋白的功能动力学
Methods Enzymol. 2007;423:149-65. doi: 10.1016/S0076-6879(07)23006-X.
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The crystal structure of beryllofluoride Spo0F in complex with the phosphotransferase Spo0B represents a phosphotransfer pretransition state.与磷酸转移酶Spo0B复合的铍氟化物Spo0F的晶体结构代表了一种磷酸转移前过渡态。
J Bacteriol. 2006 Jul;188(13):4970-7. doi: 10.1128/JB.00160-06.
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Structural classification of bacterial response regulators: diversity of output domains and domain combinations.细菌应答调节因子的结构分类：输出结构域及结构域组合的多样性
J Bacteriol. 2006 Jun;188(12):4169-82. doi: 10.1128/JB.01887-05.
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Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein.传感组氨酸激酶蛋白整个胞质部分的结构
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Keeping signals straight in phosphorelay signal transduction.在磷酸化信号转导中保持信号的清晰准确。
J Bacteriol. 2001 Sep;183(17):4941-9. doi: 10.1128/JB.183.17.4941-4949.2001.
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Histidine kinases and response regulator proteins in two-component signaling systems.双组分信号系统中的组氨酸激酶和反应调节蛋白。
Trends Biochem Sci. 2001 Jun;26(6):369-76. doi: 10.1016/s0968-0004(01)01852-7.
9
A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction.被困在晶格中的两种磷酰化中继蛋白之间的短暂相互作用揭示了信号转导中分子识别和磷转移的机制。
Structure. 2000 Aug 15;8(8):851-62. doi: 10.1016/s0969-2126(00)00174-x.
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Two-component and phosphorelay signal transduction.双组分及磷酸化信号转导
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通过协方差分析确定的双组分信号系统蛋白质-蛋白质界面处的协同进化运动。

Co-evolving motions at protein-protein interfaces of two-component signaling systems identified by covariance analysis.

作者信息

Szurmant Hendrik, Bobay Benjamin G, White Robert A, Sullivan Daniel M, Thompson Richele J, Hwa Terence, Hoch James A, Cavanagh John

机构信息

Division of Cellular Biology, Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California 92037, USA.

出版信息

Biochemistry. 2008 Jul 29;47(30):7782-4. doi: 10.1021/bi8009604. Epub 2008 Jun 28.

DOI:10.1021/bi8009604
PMID:18588317
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2830073/
Abstract

Short-lived protein interactions determine signal transduction specificity among genetically amplified, structurally identical two-component signaling systems. Interacting protein pairs evolve recognition precision by varying residues at specific positions in the interaction surface consistent with constraints of charge, size, and chemical properties. Such positions can be detected by covariance analyses of two-component protein databases. Here, covariance is shown to identify a cluster of co-evolving dynamic residues in two-component proteins. NMR dynamics and structural studies of both wild-type and mutant proteins in this cluster suggest that motions serve to precisely arrange the site of phosphoryl transfer within the complex.

摘要

短寿命的蛋白质相互作用决定了基因扩增、结构相同的双组分信号系统之间的信号转导特异性。相互作用的蛋白质对通过改变相互作用表面特定位置的残基来提高识别精度，这些残基的改变要符合电荷、大小和化学性质的限制。通过对双组分蛋白质数据库进行协方差分析可以检测到这些位置。在此，协方差分析显示能够识别双组分蛋白质中一组共同进化的动态残基。对该簇中野生型和突变型蛋白质的核磁共振动力学和结构研究表明，动态变化有助于精确排列复合物内磷酸转移的位点。