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4QTS

Crystal structure of Csm3-Csm4 subcomplex in the type III-A CRISPR-Cas interference complex

Summary for 4QTS
Entry DOI10.2210/pdb4qts/pdb
DescriptorCRISPR type III-associated RAMP protein Csm4, CRISPR type III-associated RAMP protein Csm3, ZINC ION (3 entities in total)
Functional Keywordscrispr-associated protein, ferredoxin-like fold, type iii-a crispr-cas system, rna binding protein
Biological sourceMethanocaldococcus jannaschii DSM 2661
More
Total number of polymer chains4
Total formula weight148731.35
Authors
Numata, T.,Inanaga, H.,Osawa, T. (deposition date: 2014-07-09, release date: 2014-12-24, Last modification date: 2024-05-29)
Primary citationNumata, T.,Inanaga, H.,Sato, C.,Osawa, T.
Crystal structure of the Csm3-Csm4 subcomplex in the type III-A CRISPR-Cas interference complex.
J.Mol.Biol., 427:259-273, 2015
Cited by
PubMed Abstract: Clustered, regularly interspaced, short palindromic repeat (CRISPR) loci play a pivotal role in the prokaryotic host defense system against invading genetic materials. The CRISPR loci are transcribed to produce CRISPR RNAs (crRNAs), which form interference complexes with CRISPR-associated (Cas) proteins to target the invading nucleic acid for degradation. The interference complex of the type III-A CRISPR-Cas system is composed of five Cas proteins (Csm1-Csm5) and a crRNA, and targets invading DNA. Here, we show that the Csm1, Csm3, and Csm4 proteins from Methanocaldococcus jannaschii form a stable subcomplex. We also report the crystal structure of the M. jannaschii Csm3-Csm4 subcomplex at 3.1Å resolution. The complex structure revealed the presence of a basic concave surface around their interface, suggesting the RNA and/or DNA binding ability of the complex. A gel retardation analysis showed that the Csm3-Csm4 complex binds single-stranded RNA in a non-sequence-specific manner. Csm4 structurally resembles Cmr3, a component of the type III-B CRISPR-Cas interference complex. Based on bioinformatics, we constructed a model structure of the Csm1-Csm4-Csm3 ternary complex, which provides insights into its role in the Csm interference complex.
PubMed: 25451598
DOI: 10.1016/j.jmb.2014.09.029
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.105 Å)
Structure validation

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