The structure of I-Crel, a group I intron-encoded homing endonuclease.
|Title||The structure of I-Crel, a group I intron-encoded homing endonuclease.|
|Publication Type||Journal Article|
|Year of Publication||1997|
|Authors||Heath PJ, Stephens KM, Monnat RJ, Stoddard BL|
|Journal||Nature structural biology|
|Date Published||1997 Jun|
|Keywords||Amino Acid Sequence, Binding Sites, Conserved Sequence, Crystallography, X-Ray, Deoxyribonuclease EcoRI, Deoxyribonucleases, Type II Site-Specific, Dimerization, DNA, DNA Restriction Enzymes, Eukaryotic Cells, Introns, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Folding, Recombinant Proteins, Substrate Specificity|
The structure of I-Crel provides the first view of a protein encoded by a gene within an intron. This endonuclease recognizes a long DNA site approximately 20 base pairs in length and facilitates the lateral transfer of that intron. The protein exhibits a DNA-binding surface consisting of four antiparallel beta-strands that form a 20 A wide groove which is over 70 A long. The architecture of this fold is different from that of the TATA binding protein, TBP, which also contains an antiparallel beta-saddle. The conserved LAGLIDADG motif, which is found in many mobile intron endonucleases, maturases and inteins, forms a novel helical interface and contributes essential residues to the active site.
|Alternate Journal||Nat. Struct. Biol.|