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Structure of Csm2 elucidates the relationship between small subunits of CRISPR‐Cas effector complexes
Author(s) -
Venclovas Česlovas
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12179
Subject(s) - protein subunit , crispr , effector , dimer , thermotoga maritima , chemistry , monomer , computational biology , biology , stereochemistry , crystallography , biophysics , biochemistry , gene , escherichia coli , organic chemistry , polymer
Type I and type III CRISPR‐Cas effector complexes share similar architecture and have homologous key subunits. However, the relationship between the so‐called small subunits of these complexes remains a contentious issue. Here, it is shown that the recently solved structure of Thermotoga maritima Csm2 represents a dimer with the extensive structure swapping between monomers. Unswapping the structure generates a compact globular monomer which shares similar structure and surface properties with Cmr5, the small subunit of a related Cmr complex. Detailed analysis of available structures of small subunits reveals that they all have a common fold suggesting their common origin.