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6NBT

CRISPR Complex Subunit Csm3 from Staphylococcus epidermidis RP62a

Summary for 6NBT
Entry DOI10.2210/pdb6nbt/pdb
DescriptorCRISPR-associated protein, CALCIUM ION, SAMARIUM (III) ION, ... (4 entities in total)
Functional Keywordscrispr, rna binding, rna recognition motif, samarium (iii) chloride, rna binding protein
Biological sourceStaphylococcus epidermidis (strain ATCC 35984 / RP62A)
Total number of polymer chains2
Total formula weight56099.68
Authors
Dorsey, B.W.,Mondragon, A. (deposition date: 2018-12-10, release date: 2019-02-13, Last modification date: 2024-10-23)
Primary citationDorsey, 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: 30759237
DOI: 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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