细菌解旋酶-引发酶相互作用：一种常见的结构/功能模块。
The bacterial helicase-primase interaction: a common structural/functional module.
作者信息
Soultanas Panos
机构信息
Centre for Biomolecular Sciences, School of Chemistry, University of Nottingham, Nottingham NG7 2RD, UK.
出版信息
Structure. 2005 Jun;13(6):839-44. doi: 10.1016/j.str.2005.04.006.
Abstract
The lack of a high-resolution structure for the bacterial helicase-primase complex and the fragmented structural information for the individual proteins have been hindering our detailed understanding of this crucial binary protein interaction. Two new structures for the helicase-interacting domain of the bacterial primases from Escherichia coli and Bacillus stearothermophilus have recently been solved and both revealed a unique and surprising structural similarity to the amino-terminal domain of the helicase itself. In this minireview, the current data are discussed and important new structural and functional aspects of the helicase-primase interaction are highlighted. An attractive structural model with direct biological significance for the function of this complex and also for the development of new antibacterial compounds is examined.
摘要
细菌解旋酶-引发酶复合物缺乏高分辨率结构，且单个蛋白质的结构信息支离破碎，这一直阻碍着我们对这种关键的二元蛋白质相互作用的详细理解。最近已解析出大肠杆菌和嗜热脂肪芽孢杆菌的细菌引发酶与解旋酶相互作用结构域的两个新结构，二者均显示出与解旋酶自身氨基末端结构域独特且惊人的结构相似性。在这篇小型综述中，我们讨论了当前数据，并强调了解旋酶-引发酶相互作用的重要新结构和功能方面。我们研究了一个对该复合物功能以及新抗菌化合物开发具有直接生物学意义的引人注目的结构模型。
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1
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2
Inhibiting protein-protein interactions using designed molecules.利用设计的分子抑制蛋白质-蛋白质相互作用。
Curr Opin Struct Biol. 2005 Feb;15(1):31-4. doi: 10.1016/j.sbi.2005.01.005.
3
Crystal and solution structures of the helicase-binding domain of Escherichia coli primase.大肠杆菌引发酶解旋酶结合结构域的晶体结构与溶液结构
J Biol Chem. 2005 Mar 25;280(12):11495-504. doi: 10.1074/jbc.M412645200. Epub 2005 Jan 12.
4
Protein-protein interactions; coupling of structurally conserved residues and of hot spots across interfaces. Implications for docking.蛋白质-蛋白质相互作用；跨界面的结构保守残基和热点的耦合。对接的意义。
Structure. 2004 Jun;12(6):1027-38. doi: 10.1016/j.str.2004.04.009.
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6
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