6KDV

Crystal structure of TtCas1-DNA complex

6KDV の概要

• エントリーDOI: 10.2210/pdb6kdv/pdb
• 分子名称: CRISPR-associated endonuclease Cas1 2, DNA (5'-D(*GP*AP*GP*TP*CP*GP*AP*TP*GP*CP*TP*GP*GP*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3'), DNA (5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*CP*CP*AP*GP*CP*AP*TP*CP*GP*AP*CP*TP*C)-3') (3 entities in total)
• 機能のキーワード: crispr, cas1, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 172054.89

構造登録者

Wang, Y.L.,Li, J.Z.,Yang, J.,Wang, J.Y. (登録日: 2019-07-02, 公開日: 2019-12-18, 最終更新日: 2024-11-06)

主引用文献

Yang, J.,Li, J.,Wang, J.,Sheng, G.,Wang, M.,Zhao, H.,Yang, Y.,Wang, Y.
Crystal structure of Cas1 in complex with branched DNA.
Sci China Life Sci, 63:516-528, 2020

PubMed Abstract: Cas1 is a key component of the CRISPR adaptation complex, which captures and integrates foreign DNA into the CRISPR array, resulting in the generation of new spacers. We have determined crystal structures of Thermus thermophilus Cas1 involved in new spacer acquisition both in complex with branched DNA and in the free state. Cas1 forms an asymmetric dimer without DNA. Conversely, two asymmetrical dimers bound to two branched DNAs result in the formation of a DNA-mediated tetramer, dimer of structurally asymmetrical dimers, in which the two subunits markedly present different conformations. In the DNA binding complex, the N-terminal domain adopts different orientations with respect to the C-terminal domain in the two monomers that form the dimer. Substrate binding triggers a conformational change in the loop 164-177 segment. This loop is also involved in the 3' fork arm and 5' fork arm strand recognition in monomer A and B, respectively. This study provides important insights into the molecular mechanism of new spacer adaptation.

PubMed: 31792780
DOI: 10.1007/s11427-019-9827-x

実験手法

X-RAY DIFFRACTION (3.11 Å)