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1ln0
From Proteopedia
| 1ln0, resolution 2.00Å () | |||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Structure of the Catalytic Domain of Homing Endonuclease I-TevI
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1ln0 is a 2 chain structure with sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
See Also
Reference
- Van Roey P, Meehan L, Kowalski JC, Belfort M, Derbyshire V. Catalytic domain structure and hypothesis for function of GIY-YIG intron endonuclease I-TevI. Nat Struct Biol. 2002 Nov;9(11):806-11. PMID:12379841 doi:10.1038/nsb853
