1ln0
From Proteopedia
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'''Structure of the Catalytic Domain of Homing Endonuclease I-TevI''' | '''Structure of the Catalytic Domain of Homing Endonuclease I-TevI''' | ||
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[[Category: Meehan, L.]] | [[Category: Meehan, L.]] | ||
[[Category: Roey, P Van.]] | [[Category: Roey, P Van.]] | ||
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Revision as of 21:04, 2 May 2008
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 Enterobacteria phage t4. 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 Sat May 3 00:04:45 2008
