Structural highlights
Function
[DNE1_CHLRE] Endonuclease involved in group I intron homing. Recognizes and cleaves a 19-24 bp palindromic DNA site.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
References
- ↑ Heath PJ, Stephens KM, Monnat RJ Jr, Stoddard BL. The structure of I-Crel, a group I intron-encoded homing endonuclease. Nat Struct Biol. 1997 Jun;4(6):468-76. PMID:9187655
