4H79

Crystal structure of CasB from Thermobifida fusca

Summary for 4H79

• Entry DOI: 10.2210/pdb4h79/pdb
• Descriptor: CRISPR-associated protein, Cse2 family, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: crispr, cascade, casb, crispr-assoicated protein, nucleic acid binding protein, dna binding protein
• Biological source: Thermobifida fusca
• Total number of polymer chains: 1
• Total formula weight: 24807.02

Authors

Ke, A.,Nam, K.H. (deposition date: 2012-09-20, release date: 2012-10-03, Last modification date: 2023-09-20)

Primary citation

Nam, K.H.,Huang, Q.,Ke, A.
Nucleic acid binding surface and dimer interface revealed by CRISPR-associated CasB protein structures.
Febs Lett., 586:3956-3961, 2012

PubMed Abstract: The CRISPR system is an adaptive RNA-based microbial immune system against invasive genetic elements. CasB is an essential protein component in Type I-E Cascade. Here, we characterize CasB proteins from three different organisms as non-specific nucleic acid binding proteins. The Thermobifida fusca CasB crystal structure reveals conserved positive surface charges, which we show are important for its nucleic acid binding function. EM docking reveals that CasB dimerization aligns individual nucleic acid binding surfaces into a curved, elongated binding surface inside Type I-E Cascade, consistent with the putative functions of CasB in ds-DNA recruitment and crRNA-DNA duplex formation steps.

PubMed: 23079036
DOI: 10.1016/j.febslet.2012.09.041

Experimental method

X-RAY DIFFRACTION (1.9 Å)