期刊
JOURNAL OF STRUCTURAL BIOLOGY
卷 178, 期 3, 页码 350-362出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2012.04.006
关键词
CRISPR; Spacer integration; X-ray crystallography; MD-simulation; DNA binding
资金
- Deutsche Forschungsgemeinschaft (DFG) [PU 435/1-1]
- Heinrich Heine University
- initiative Fit for Excellence at the Heinrich Heine University
- Protein Production Facility-Crystal and X-ray Facility
The prokaryotic immune system, CRISPR, confers an adaptive and inheritable defense mechanism against invasion by mobile genetic elements. Guided by small CRISPR RNAs (crRNAs), a diverse family of CRISPR-associated (Cas) proteins mediates the targeting and inactivation of foreign DNA. Here, we demonstrate that Csn2, a Cas protein likely involved in spacer integration, forms a tetramer in solution and structurally possesses a ring-like structure. Furthermore, co-purified Ca2+ was found important for the DNA binding property of Csn2, which contains a helicase fold, with highly conserved DxD and RR motifs found throughout Csn2 proteins. We could verify that Csn2 binds ds-DNA. In addition molecular dynamics simulations suggested a Csn2 conformation that can sit on the DNA helix and binds DNA in a groove on the outside of the ring. (c) 2012 Elsevier Inc. All rights reserved.
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