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 |
| Volume | 4 |
| Issue | 6 |
| Pagination | 468-76 |
| Date Published | 1997 Jun |
| ISSN | 1072-8368 |
| 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 |
| Abstract | 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. |
| PubMed ID | 9187655 |