6NBT
CRISPR Complex Subunit Csm3 from Staphylococcus epidermidis RP62a
Summary for 6NBT
| Entry DOI | 10.2210/pdb6nbt/pdb |
| Descriptor | CRISPR-associated protein, CALCIUM ION, SAMARIUM (III) ION, ... (4 entities in total) |
| Functional Keywords | crispr, rna binding, rna recognition motif, samarium (iii) chloride, rna binding protein |
| Biological source | Staphylococcus epidermidis (strain ATCC 35984 / RP62A) |
| Total number of polymer chains | 2 |
| Total formula weight | 56099.68 |
| Authors | Dorsey, B.W.,Mondragon, A. (deposition date: 2018-12-10, release date: 2019-02-13, Last modification date: 2024-10-23) |
| Primary citation | Dorsey, B.W.,Huang, L.,Mondragon, A. Structural organization of a Type III-A CRISPR effector subcomplex determined by X-ray crystallography and cryo-EM. Nucleic Acids Res., 47:3765-3783, 2019 Cited by PubMed Abstract: Clustered regularly interspaced short palindromic repeats (CRISPR) and their associated Cas proteins provide an immune-like response in many prokaryotes against extraneous nucleic acids. CRISPR-Cas systems are classified into different classes and types. Class 1 CRISPR-Cas systems form multi-protein effector complexes that includes a guide RNA (crRNA) used to identify the target for destruction. Here we present crystal structures of Staphylococcus epidermidis Type III-A CRISPR subunits Csm2 and Csm3 and a 5.2 Å resolution single-particle cryo-electron microscopy (cryo-EM) reconstruction of an in vivo assembled effector subcomplex including the crRNA. The structures help to clarify the quaternary architecture of Type III-A effector complexes, and provide details on crRNA binding, target RNA binding and cleavage, and intermolecular interactions essential for effector complex assembly. The structures allow a better understanding of the organization of Type III-A CRISPR effector complexes as well as highlighting the overall similarities and differences with other Class 1 effector complexes. PubMed: 30759237DOI: 10.1093/nar/gkz079 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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