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1mk0
From Proteopedia
(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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| - | [[Image:1mk0.jpg|left|200px]]<br /><applet load="1mk0" size=" | + | [[Image:1mk0.jpg|left|200px]]<br /><applet load="1mk0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mk0, resolution 1.60Å" /> | caption="1mk0, resolution 1.60Å" /> | ||
'''catalytic domain of intron endonuclease I-TevI, E75A mutant'''<br /> | '''catalytic domain of intron endonuclease I-TevI, E75A mutant'''<br /> | ||
==Overview== | ==Overview== | ||
| - | I-TevI, a member of the GIY-YIG family of homing endonucleases, consists | + | 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== | ==About this Structure== | ||
| - | 1MK0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with CIT and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1MK0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with <scene name='pdbligand=CIT:'>CIT</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MK0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Belfort, M.]] | [[Category: Belfort, M.]] | ||
[[Category: Derbyshire, V.]] | [[Category: Derbyshire, V.]] | ||
| - | [[Category: Kowalski, J | + | [[Category: Kowalski, J C.]] |
[[Category: Meehan, L.]] | [[Category: Meehan, L.]] | ||
| - | [[Category: Roey, P | + | [[Category: Roey, P Van.]] |
[[Category: BME]] | [[Category: BME]] | ||
[[Category: CIT]] | [[Category: CIT]] | ||
[[Category: alpha/beta fold; catalytic domain; dna-binding surface]] | [[Category: alpha/beta fold; catalytic domain; dna-binding surface]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:01 2008'' |
Revision as of 11:56, 21 February 2008
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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 and 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
Page seeded by OCA on Thu Feb 21 13:56:01 2008
