1mk0
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(New page: 200px<br /><applet load="1mk0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mk0, resolution 1.60Å" /> '''catalytic domain of ...)
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Revision as of 19:21, 20 November 2007
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catalytic domain of intron endonuclease I-TevI, E75A mutant
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
1MK0 is a Single protein structure of sequence from Bacteriophage t4 with CIT and BME as ligands. 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
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