1ln0: Difference between revisions
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[[Image:1ln0.gif|left|200px]] | [[Image:1ln0.gif|left|200px]] | ||
'''Structure of the Catalytic Domain of Homing Endonuclease I-TevI''' | {{Structure | ||
|PDB= 1ln0 |SIZE=350|CAPTION= <scene name='initialview01'>1ln0</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Structure of the Catalytic Domain of Homing Endonuclease I-TevI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LN0 is a [ | 1LN0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LN0 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12379841 12379841] | ||
[[Category: Bacteriophage t4]] | [[Category: Bacteriophage t4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alpha/beta fold]] | [[Category: alpha/beta fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:32:43 2008'' | ||
Revision as of 10:32, 20 March 2008
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| 1ln0, resolution 2.0Å | |||||||||||||
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| Ligands: | SO4 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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