3OQ2
Structure of a CRISPR associated protein Cas2 from Desulfovibrio vulgaris
Summary for 3OQ2
| Entry DOI | 10.2210/pdb3oq2/pdb |
| Descriptor | CRISPR-associated protein Cas2, SODIUM ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (7 entities in total) |
| Functional Keywords | ferredoxin fold, crispr, immune system |
| Biological source | Desulfovibrio vulgaris |
| Total number of polymer chains | 2 |
| Total formula weight | 25130.62 |
| Authors | Samai, P.,Smith, P.,Shuman, S. (deposition date: 2010-09-02, release date: 2010-12-22, Last modification date: 2024-02-21) |
| Primary citation | Samai, P.,Smith, P.,Shuman, S. Structure of a CRISPR-associated protein Cas2 from Desulfovibrio vulgaris. Acta Crystallogr.,Sect.F, 66:1552-1556, 2010 Cited by 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: 21139194DOI: 10.1107/S1744309110039801 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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