Publication Abstract from PubMed
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.
The structure of I-Crel, a group I intron-encoded homing endonuclease.,Heath PJ, Stephens KM, Monnat RJ Jr, Stoddard BL Nat Struct Biol. 1997 Jun;4(6):468-76. PMID:9187655[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
