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• W4317492045 endingPage "140900" @default.
• W4317492045 startingPage "140900" @default.
• W4317492045 abstract "Clustered regularly interspaced short palindromic repeats (CRISPR) in many prokaryotes functions as an adaptive immune system against mobile genetic elements. A heterologous ribonucleoprotein silencing complex composed of CRISPR-associated (Cas) proteins and a CRISPR RNA (crRNA) neutralizes the incoming mobile genetic elements. The type I and III silencing complexes commonly include a protein-helical backbone of several copies of identical subunits, for example, Cas7 in the type I silencing complex. In this study, we structurally characterized type I-B Cas7 (Csh2 from Thermobaculum terrenum; TterCsh2). The revealed crystal structure of TterCsh2 shows a typical glove-like architecture of Cas7, which consists of a palm, a thumb, and a finger domain. Csh2 proteins have 5 conserved sequence motifs that are arranged to form a presumable crRNA-binding site in the TterCsh2 structure. This crRNA binding site of TterCsh2 is structurally and potentially comparable to those observed in helix-forming Cas7 structures in other sub-types. Analysis of the reported Cas7 structures and their sequences suggests that Cas7s can be divided into at least two sub-classes. These data will broaden our understanding on the Cascade complex of CRISPR/Cas systems." @default.
• W4317492045 created "2023-01-20" @default.
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• W4317492045 date "2023-05-01" @default.
• W4317492045 modified "2023-10-16" @default.
• W4317492045 title "Structural characterization of the type I-B CRISPR Cas7 from Thermobaculum terrenum" @default.
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• W4317492045 doi "https://doi.org/10.1016/j.bbapap.2023.140900" @default.
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