1ln0
From Proteopedia
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Structure of the Catalytic Domain of Homing Endonuclease I-TevI
Overview
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.
About this Structure
1LN0 is a Single protein structure of sequence from Bacteriophage t4 with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Catalytic domain structure and hypothesis for function of GIY-YIG intron endonuclease I-TevI., Van Roey P, Meehan L, Kowalski JC, Belfort M, Derbyshire V, Nat Struct Biol. 2002 Nov;9(11):806-11. PMID:12379841
Page seeded by OCA on Tue Nov 20 20:41:19 2007
