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8D97

Apo gRAMP

Summary for 8D97
Entry DOI10.2210/pdb8d97/pdb
EMDB information27257
DescriptorRAMP superfamily protein, RNA (42-MER), ZINC ION (3 entities in total)
Functional Keywordscrispr, gramp, rna binding protein, rna binding protein-rna complex, rna binding protein/rna
Biological sourceCandidatus Scalindua brodae
More
Total number of polymer chains2
Total formula weight197908.93
Authors
Hu, C.,Nam, K.H.,Schuler, G.,Ke, A. (deposition date: 2022-06-09, release date: 2023-06-14, Last modification date: 2024-11-20)
Primary citationHu, C.,van Beljouw, S.P.B.,Nam, K.H.,Schuler, G.,Ding, F.,Cui, Y.,Rodriguez-Molina, A.,Haagsma, A.C.,Valk, M.,Pabst, M.,Brouns, S.J.J.,Ke, A.
Craspase is a CRISPR RNA-guided, RNA-activated protease.
Science, 377:1278-1285, 2022
Cited by
PubMed Abstract: The CRISPR-Cas type III-E RNA-targeting effector complex gRAMP/Cas7-11 is associated with a caspase-like protein (TPR-CHAT/Csx29) to form Craspase (CRISPR-guided caspase). Here, we use cryo-electron microscopy snapshots of Craspase to explain its target RNA cleavage and protease activation mechanisms. Target-guide pairing extending into the 5' region of the guide RNA displaces a gating loop in gRAMP, which triggers an extensive conformational relay that allosterically aligns the protease catalytic dyad and opens an amino acid side-chain-binding pocket. We further define Csx30 as the endogenous protein substrate that is site-specifically proteolyzed by RNA-activated Craspase. This protease activity is switched off by target RNA cleavage by gRAMP and is not activated by RNA targets containing a matching protospacer flanking sequence. We thus conclude that Craspase is a target RNA-activated protease with self-regulatory capacity.
PubMed: 36007061
DOI: 10.1126/science.add5064
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.8 Å)
Structure validation

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