ATP Hydrolysis in the RecA-DNA Filament Promotes Structural Changes at the Protein-DNA Interface

被引：9

作者：

Reymer, Anna ^{[1
]}

Babik, Sandor ^{[2
]}

Takahashi, Masayuki ^{[3
]}

Norden, Bengt ^{[2
]}

Beke-Somfai, Tamas ^{[2
,4
]}

机构：

[1] Gothenburg Univ, Dept Chem & Mol Biol, SE-40530 Gothenburg, Sweden

[2] Chalmers, Dept Chem & Biol Engn, Phys Chem, SE-41296 Gothenburg, Sweden

[3] Tokyo Inst Technol, Sch Biosci & Biotechnol, Meguro Ku, Tokyo 1528550, Japan

[4] Hungarian Acad Sci, Inst Mat Chem, Res Ctr Nat Sci, H-1117 Budapest, Hungary

来源：

BIOCHEMISTRY | 2015年 / 54卷 / 30期

基金：

瑞典研究理事会;

关键词：

ESCHERICHIA-COLI RECA; HOMOLOGOUS RECOMBINATION; MECHANISM; SYNTHASE; MOTOR; CATALYSIS; SYSTEMS; SITES;

D O I：

10.1021/acs.biochem.5b00614

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

To address the mechanistic roles of ATP hydrolysis in RecA-promoted strand exchange reaction in homologous recombination, quantum mechanical calculations are performed on key parts of the RecA-DNA complex. We find that ATP hydrolysis may induce changes at the protein-DNA interface, resulting in the rearrangement of the hydrogen bond network connecting the ATP and the DNA binding sites.

引用

页码：4579 / 4582

页数：4

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