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-Structure paper
タイトル | ATP-mediated conformational changes in the RecA filament. |
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ジャーナル・号・ページ | Structure, Vol. 11, Issue 2, Page 187-196, Year 2003 |
掲載日 | 2003年8月27日 |
![]() | Margaret S VanLoock / Xiong Yu / Shixin Yang / Alex L Lai / Claudia Low / Michael J Campbell / Edward H Egelman / ![]() |
PubMed 要旨 | The crystal structure of the E. coli RecA protein was solved more than 10 years ago, but it has provided limited insight into the mechanism of homologous genetic recombination. Using electron ...The crystal structure of the E. coli RecA protein was solved more than 10 years ago, but it has provided limited insight into the mechanism of homologous genetic recombination. Using electron microscopy, we have reconstructed five different states of RecA-DNA filaments. The C-terminal lobe of the RecA protein is modulated by the state of the distantly bound nucleotide, and this allosteric coupling can explain how mutations and truncations of this C-terminal lobe enhance RecA's activity. A model generated from these reconstructions shows that the nucleotide binding core is substantially rotated from its position in the RecA crystal filament, resulting in ATP binding between subunits. This simple rotation can explain the large cooperativity in ATP hydrolysis observed for RecA-DNA filaments. |
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手法 | EM (らせん対称) |
解像度 | 20 Å |
構造データ | ![]() PDB-1n03: |
化合物 | ![]() ChemComp-ADP: |
由来 |
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![]() | DNA BINDING PROTEIN / helical polymer |