Structure of a CRISPR-associated protein Cas2 from Desulfovibrio vulgaris Journal Article
| Authors: | Samai, P.; Smith, P.; Shuman, S. |
| Article Title: | Structure of a CRISPR-associated protein Cas2 from Desulfovibrio vulgaris |
| 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 ΒΒΒΒ 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. © 2010 International Union of Crystallography. All rights reserved. |
| Keywords: | cas2; crispr-associated proteins; desulfovibrio vulgaris |
| Journal Title: | Acta Crystallographica Section F: Structural Biology Communications |
| Volume: | 66 |
| Issue: | 12 |
| ISSN: | 2053-230X |
| Publisher: | Wiley Blackwell |
| Date Published: | 2010-12-01 |
| Start Page: | 1552 |
| End Page: | 1556 |
| Language: | English |
| DOI: | 10.1107/s1744309110039801 |
| PROVIDER: | scopus |
| PMCID: | PMC2998353 |
| PUBMED: | 21139194 |
| DOI/URL: | |
| Notes: | --- - "Export Date: 20 April 2011" - "Source: Scopus" |
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