3OQ2

Structure of a CRISPR associated protein Cas2 from Desulfovibrio vulgaris

3OQ2 の概要

• エントリーDOI: 10.2210/pdb3oq2/pdb
• 分子名称: CRISPR-associated protein Cas2, SODIUM ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (7 entities in total)
• 機能のキーワード: ferredoxin fold, crispr, immune system
• 由来する生物種: Desulfovibrio vulgaris
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25130.62

構造登録者

Samai, P.,Smith, P.,Shuman, S. (登録日: 2010-09-02, 公開日: 2010-12-22, 最終更新日: 2024-02-21)

主引用文献

Samai, P.,Smith, P.,Shuman, S.
Structure of a CRISPR-associated protein Cas2 from Desulfovibrio vulgaris.
Acta Crystallogr.,Sect.F, 66:1552-1556, 2010

PubMed Abstract: CRISPRs (clustered regularly interspaced short palindromic repeats) provide bacteria and archaea with RNA-guided acquired immunity to invasive DNAs. CRISPR-associated (Cas) proteins carry out the immune effector functions. Cas2 is a universal component of the CRISPR system. Here, a 1.35 Å resolution crystal structure of Cas2 from the bacterium Desulfovibrio vulgaris (DvuCas2) is reported. DvuCas2 is a homodimer, with each protomer consisting of an N-terminal βαββαβ ferredoxin fold (amino acids 1-78) to which is appended a C-terminal segment (amino acids 79-102) that includes a short 3(10)-helix and a fifth β-strand. The β5 strands align with the β4 strands of the opposite protomers, resulting in two five-stranded antiparallel β-sheets that form a sandwich at the dimer interface. The DvuCas2 dimer is stabilized by a distinctive network of hydrophilic cross-protomer side-chain interactions.

PubMed: 21139194
DOI: 10.1107/S1744309110039801

実験手法

X-RAY DIFFRACTION (1.35 Å)