Structural Insight Into the Function of DnaB Helicase in Bacterial DNA Replication.

IF 3.2 4区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Proteins-Structure Function and Bioinformatics Pub Date : 2025-02-01 Epub Date: 2024-09-04 DOI:10.1002/prot.26746

Zhiming Zhang, Jiang Chen, Maochun Yao, Ganggang Wang

引用次数: 0

Abstract

In bacteria, chromosome replication is achieved by the coordinations of more than a dozen replisome enzymes. Replication initiation protein DnaA melts DNA duplex at replication origin (oriC) and forms a replication bubble, followed by loading of helicase DnaB with the help of loader protein DnaC. Then the DnaB helicase unwinds the dsDNA and supports the priming of DnaG and the polymerizing of DNA polymerase. The DnaB helicase functions as a platform coupling unwinding, priming, and polymerizing events. The multiple roles of DnaB helicase are underlined by its distinctive architecture and dynamics conformations. In this review, we will discuss the assembling of DnaB hexamer and the conformational changes upon binding of various partners, DnaB in states of closed dilated (CD), closed constricted (CC), closed helical (CH), and open helical (OH) are discussed. These multiple interfaces among DnaB and partners are potential targets for inhibitors design and novel peptide antibiotics development.

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从结构上揭示 DnaB 螺旋酶在细菌 DNA 复制中的功能

在细菌中，染色体的复制是由十几种复制酶协同完成的。复制起始蛋白 DnaA 在复制原点（oriC）熔化 DNA 双链，形成复制泡，然后在装载蛋白 DnaC 的帮助下装载螺旋酶 DnaB。然后，DnaB 螺旋酶解开 dsDNA，支持 DnaG 的引物和 DNA 聚合酶的聚合。DnaB 螺旋酶作为一个平台，将解旋、引物和聚合事件耦合在一起。DnaB 螺旋酶的独特结构和动态构象凸显了它的多重作用。在这篇综述中，我们将讨论 DnaB 六聚体的组装以及与各种伙伴结合后的构象变化，并讨论 DnaB 在闭合扩张（CD）、闭合收缩（CC）、闭合螺旋（CH）和开放螺旋（OH）状态下的构象变化。DnaB 与合作伙伴之间的这些多重界面是抑制剂设计和新型多肽抗生素开发的潜在目标。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Proteins-Structure Function and Bioinformatics 生物-生化与分子生物学

CiteScore

5.90

自引率

3.40%

发文量

172

审稿时长

3 months

期刊介绍： PROTEINS : Structure, Function, and Bioinformatics publishes original reports of significant experimental and analytic research in all areas of protein research: structure, function, computation, genetics, and design. The journal encourages reports that present new experimental or computational approaches for interpreting and understanding data from biophysical chemistry, structural studies of proteins and macromolecular assemblies, alterations of protein structure and function engineered through techniques of molecular biology and genetics, functional analyses under physiologic conditions, as well as the interactions of proteins with receptors, nucleic acids, or other specific ligands or substrates. Research in protein and peptide biochemistry directed toward synthesizing or characterizing molecules that simulate aspects of the activity of proteins, or that act as inhibitors of protein function, is also within the scope of PROTEINS. In addition to full-length reports, short communications (usually not more than 4 printed pages) and prediction reports are welcome. Reviews are typically by invitation; authors are encouraged to submit proposed topics for consideration.