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-Structure paper
タイトル | FtsK in motion reveals its mechanism for double-stranded DNA translocation. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 117, Issue 25, Page 14202-14208, Year 2020 |
掲載日 | 2020年6月23日 |
著者 | Nicolas L Jean / Trevor J Rutherford / Jan Löwe / |
PubMed 要旨 | FtsK protein contains a fast DNA motor that is involved in bacterial chromosome dimer resolution. During cell division, FtsK translocates double-stranded DNA until both recombination sites are ...FtsK protein contains a fast DNA motor that is involved in bacterial chromosome dimer resolution. During cell division, FtsK translocates double-stranded DNA until both recombination sites are placed at mid cell for subsequent dimer resolution. Here, we solved the 3.6-Å resolution electron cryo-microscopy structure of the motor domain of FtsK while translocating on its DNA substrate. Each subunit of the homo-hexameric ring adopts a unique conformation and one of three nucleotide states. Two DNA-binding loops within four subunits form a pair of spiral staircases within the ring, interacting with the two DNA strands. This suggests that simultaneous conformational changes in all ATPase domains at each catalytic step generate movement through a mechanism related to filament treadmilling. While the ring is only rotating around the DNA slowly, it is instead the conformational states that rotate around the ring as the DNA substrate is pushed through. |
リンク | Proc Natl Acad Sci U S A / PubMed:32513722 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.65 - 4.91 Å |
構造データ | EMDB-10399, PDB-6t8b: EMDB-10400, PDB-6t8g: EMDB-10402, PDB-6t8o: EMDB-10403: EMDB-10404: EMDB-10405: |
化合物 | ChemComp-AGS: ChemComp-MG: ChemComp-ADP: |
由来 |
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キーワード | DNA BINDING PROTEIN / DNA translocation / DNA motor / RecA fold / Divisome |