1LN0

Structure of the Catalytic Domain of Homing Endonuclease I-TevI

Summary for 1LN0

• Entry DOI: 10.2210/pdb1ln0/pdb
• Descriptor: intron-associated endonuclease 1, SULFATE ION (3 entities in total)
• Functional Keywords: alpha/beta fold, hydrolase
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 2
• Total formula weight: 22948.08

Authors

Van Roey, P.,Meehan, L.,Kowalski, J.C.,Belfort, M.,Derbyshire, V. (deposition date: 2002-05-02, release date: 2002-10-30, Last modification date: 2024-10-30)

Primary citation

Van Roey, P.,Meehan, L.,Kowalski, J.C.,Belfort, M.,Derbyshire, V.
Catalytic domain structure and hypothesis for function of GIY-YIG intron endonuclease I-TevI.
Nat.Struct.Biol., 9:806-811, 2002

PubMed Abstract: 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.

PubMed: 12379841

Experimental method

X-RAY DIFFRACTION (2 Å)