Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase

被引：44

作者：

Biswas, Tapan ^{[1
]}

Tsodikov, Oleg V. ^{[1
]}

机构：

[1] Univ Michigan, Coll Pharm, Dept Med Chem, Ann Arbor, MI 48109 USA

来源：

FEBS JOURNAL | 2008年 / 275卷 / 12期

关键词：

crystal structure; DnaB helicase; primase; replication; tuberculosis;

D O I：

10.1111/j.1742-4658.2008.06460.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Hexameric DnaB helicase unwinds the DNA double helix during replication of genetic material in bacteria. DnaB is an essential bacterial protein; therefore, it is an important potential target for antibacterial drug discovery. We report a crystal structure of the N-terminal region of DnaB from the pathogen Mycobacterium tuberculosis (MtDnaBn), determined at 2.0 angstrom resolution. This structure provides atomic resolution details of formation of the hexameric ring of DnaB by two distinct interfaces. An extensive hydrophobic interface stabilizes a dimer of MtDnaBn by forming a four-helix bundle. The other, less extensive, interface is formed between the dimers, connecting three of them into a hexameric ring. On the basis of crystal packing interactions between MtDnaBn rings, we suggest a model of a helicase-primase complex that explains previously observed effects of DnaB mutations on DNA priming.

引用

页码：3064 / 3071

页数：8

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