1af5 | pdb_00001af5
GROUP I MOBILE INTRON ENDONUCLEASE
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Overview
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.
About this Structure
1AF5 is a Single protein structure of sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.
Reference
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
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