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Structure of a CRISPR‐associated protein Cas2 from Desulfovibrio vulgaris

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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 310‐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.
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Keywords: CRISPR‐associated proteins; Cas2; Desulfovibrio vulgaris

Document Type: Research Article

Affiliations: Molecular Biology Program, Sloan–Kettering Institute for Cancer Research, USA

Publication date: December 1, 2010

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