4N0L

Methanopyrus kandleri Csm3 crystal structure

Summary for 4N0L

• Entry DOI: 10.2210/pdb4n0l/pdb
• Descriptor: Predicted component of a thermophile-specific DNA repair system, contains a RAMP domain, ZINC ION (3 entities in total)
• Functional Keywords: rrm-like fold, crrna binding, cas/csm proteins, rna binding protein
• Biological source: Methanopyrus kandleri
• Total number of polymer chains: 2
• Total formula weight: 79374.47

Authors

Hrle, A.,Su, A.A.,Ebert, J.,Benda, C.,Conti, E.,Randau, L. (deposition date: 2013-10-02, release date: 2013-11-13, Last modification date: 2024-02-28)

Primary citation

Hrle, A.,Su, A.A.,Ebert, J.,Benda, C.,Randau, L.,Conti, E.
Structure and RNA-binding properties of the Type III-A CRISPR-associated protein Csm3.
Rna Biol., 10:1670-1678, 2013

PubMed Abstract: The prokaryotic adaptive immune system is based on the incorporation of genome fragments of invading viral genetic elements into clusters of regulatory interspaced short palindromic repeats (CRISPRs). The CRISPR loci are transcribed and processed into crRNAs, which are then used to target the invading nucleic acid for degradation. The large family of CRISPR-associated (Cas) proteins mediates this interference response. We have characterized Methanopyrus kandleri Csm3, a protein of the type III-A CRISPR-Cas complex. The 2.4 Å resolution crystal structure shows an elaborate four-domain fold organized around a core RRM-like domain. The overall architecture highlights the structural homology to Cas7, the Cas protein that forms the backbone of type I interference complexes. Csm3 binds unstructured RNAs in a sequence non-specific manner, suggesting that it interacts with the variable spacer sequence of the crRNA. The structural and biochemical data provide insights into the similarities and differences in this group of Cas proteins.

PubMed: 24157656
DOI: 10.4161/rna.26500

Experimental method

X-RAY DIFFRACTION (2.37 Å)