1LN0

Catalytic domain structure and hypothesis for function of GIY-YIG intron endonuclease I-TevI.

(2002) Nat Struct Biol 9: 806-811

• PubMed: 12379841 Search on PubMed
• DOI: https://doi.org/10.1038/nsb853
• Primary Citation of Related Structures:  
  1LN0, 1MK0


• PubMed Abstract: 
  

  I-TevI, a member of the GIY-YIG family of homing endonucleases, consists of an N-terminal catalytic domain and a C-terminal DNA-binding domain joined by a flexible linker. The GIY-YIG motif is in the N-terminal domain of I-TevI, which corresponds to a phylogenetically widespread catalytic cartridge that is often associated with mobile genetic elements. The crystal structure of the catalytic domain of I-TevI, the first of any GIY-YIG endonuclease, reveals a novel alpha/beta-fold with a central three-stranded antiparallel beta-sheet flanked by three helices. The most conserved and putative catalytic residues are located on a shallow, concave surface and include a metal coordination site. Similarities in the three-dimensional arrangement of the catalytically important residues and the cation-binding site with those of the His-Cys box endonuclease I-PpoI suggest the possibility of mechanistic relationships among these different families of homing endonucleases despite completely different folds.

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Organizational Affiliation: 

Wadsworth Center, New York State Department Health, Albany, New York 12201-0509, USA. vanroey@wadsworth.org