5DLJ
Crystal Structure of Cas-DNA-N1 complex
5DLJ の概要
エントリーDOI | 10.2210/pdb5dlj/pdb |
関連するPDBエントリー | 5DQT 5DQU 5DQZ |
分子名称 | CRISPR-associated endonuclease Cas1, 39-mer DNA N1-F, 39-mer DNA N1-R, ... (5 entities in total) |
機能のキーワード | protein-dna complex, hydrolase-dna complex, hydrolase/dna |
由来する生物種 | Escherichia coli K12 詳細 |
細胞内の位置 | Cytoplasm : Q46896 |
タンパク質・核酸の鎖数 | 8 |
化学式量合計 | 164304.00 |
構造登録者 | |
主引用文献 | Wang, J.,Li, J.,Zhao, H.,Sheng, G.,Wang, M.,Yin, M.,Wang, Y. Structural and Mechanistic Basis of PAM-Dependent Spacer Acquisition in CRISPR-Cas Systems. Cell, 163:840-853, 2015 Cited by PubMed Abstract: Bacteria acquire memory of viral invaders by incorporating invasive DNA sequence elements into the host CRISPR locus, generating a new spacer within the CRISPR array. We report on the structures of Cas1-Cas2-dual-forked DNA complexes in an effort toward understanding how the protospacer is sampled prior to insertion into the CRISPR locus. Our study reveals a protospacer DNA comprising a 23-bp duplex bracketed by tyrosine residues, together with anchored flanking 3' overhang segments. The PAM-complementary sequence in the 3' overhang is recognized by the Cas1a catalytic subunits in a base-specific manner, and subsequent cleavage at positions 5 nt from the duplex boundary generates a 33-nt DNA intermediate that is incorporated into the CRISPR array via a cut-and-paste mechanism. Upon protospacer binding, Cas1-Cas2 undergoes a significant conformational change, generating a flat surface conducive to proper protospacer recognition. Here, our study provides important structure-based mechanistic insights into PAM-dependent spacer acquisition. PubMed: 26478180DOI: 10.1016/j.cell.2015.10.008 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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