Structure of a CRISPR-associated protein Cas2 from Desulfovibrio vulgaris.
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.
Molecular Biology Program, Sloan-Kettering Institute for Cancer Research, USA.
Poulami
P
Samai
Paul
P
Smith
Stewart
S
Shuman
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D016969:Desulfovibrio vulgaris / Q000737:chemistry*; D008969:Molecular Sequence Data; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D020449:Repetitive Sequences, Amino Acid; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D010727:Phosphoric Diester Hydrolases