Fig. 3: Cryo-EM structure of gRAMPcrRNA in complex with TPR-CHAT. | Nature Communications

Fig. 3: Cryo-EM structure of gRAMPcrRNA in complex with TPR-CHAT.

From: Structural basis for the non-self RNA-activated protease activity of the type III-E CRISPR nuclease-protease Craspase

Fig. 3: Cryo-EM structure of gRAMPcrRNA in complex with TPR-CHAT.The alt text for this image may have been generated using AI.

Schematic (a) and ribbon (b) representations of cryo-EM structure of gRAMPcrRNA-TPR-CHAT complex at 2.6 Å resolution. The associate TPR-CHAT subunit is shown in surface view. c TPR-CHAT binds to Loop 2 in gRAMP. d Multiple sequence alignment of representative CHAT and separase orthologues. The conserved catalytic residues H585 and C627 are indicated by red triangles. CsbCHAT: KHE91663.1; DiCHAT: WP_124327588.1; CjcCHAT: KAA0249747.1; SmCHAT: OBJA01001127.1; FmCHAT: SESD01000293.1; GwCHAT: MGTA01000040.1; OmCHAT: PDWI01005922.1; Ct: Chaetomium thermophilum; Sc: Saccharomyces cerevisiae; Hs: Homo sapiens. Structures of bacterial TPR-CHAT (e) and human separase (PDB 7NJ1) (f) with an expanded view of the catalytic pocket. The catalytic residues are shown as red spheres. TPR, Tetratricopeptide Repeat Domain; CHAT, Caspase HetF Associated with TPRs; SPD, Separase Protease Domain.

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