8H2F

Crystal structure of DnaQ domain in complex witn TMP of Streptococcus thermophilus strain DGCC 7710

8H2F の概要

• エントリーDOI: 10.2210/pdb8h2f/pdb
• 分子名称: DnaQ, THYMIDINE-5'-PHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: nuclease, lyase
• 由来する生物種: Streptococcus thermophilus DGCC 7710
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20922.52

構造登録者

Chen, Q.,Yu, Y. (登録日: 2022-10-05, 公開日: 2023-09-13, 最終更新日: 2023-09-20)

主引用文献

Tang, D.,Jia, T.,Luo, Y.,Mou, B.,Cheng, J.,Qi, S.,Yao, S.,Su, Z.,Yu, Y.,Chen, Q.
DnaQ mediates directional spacer acquisition in the CRISPR-Cas system by a time-dependent mechanism.
Innovation (N Y), 4:100495-100495, 2023

PubMed Abstract: In the spacer acquisition stage of CRISPR-Cas immunity, spacer orientation and protospacer adjacent motif (PAM) removal are two prerequisites for functional spacer integration. Cas4 has been implicated in both processing the prespacer and determining the spacer orientation. In Cas4-lacking systems, host 3'-5' DnaQ family exonucleases were recently reported to play a Cas4-like role. However, the molecular details of DnaQ functions remain elusive. Here, we characterized the spacer acquisition of the adaptation module of the type I-E system, in which a DnaQ domain naturally fuses with Cas2. We presented X-ray crystal structures and cryo-electron microscopy structures of this adaptation module. Our biochemical data showed that DnaQ trimmed PAM-containing and PAM-deficient overhangs with different efficiencies. Based on these results, we proposed a time-dependent model for DnaQ-mediated spacer acquisition to elucidate PAM removal and spacer orientation determination in Cas4-lacking CRISPR-Cas systems.

PubMed: 37663930
DOI: 10.1016/j.xinn.2023.100495

実験手法

X-RAY DIFFRACTION (1.448 Å)