Summary information and primary citation
- PDB-id
- 1u3e; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- DNA binding protein-DNA
- Method
- X-ray (2.92 Å)
- Summary
- DNA binding and cleavage by the hnh homing endonuclease i-hmui
- Reference
- Shen BW, Landthaler M, Shub DA, Stoddard BL (2004): "DNA Binding and Cleavage by the HNH Homing Endonuclease I-HmuI." J.Mol.Biol., 342, 43-56. doi: 10.1016/j.jmb.2004.07.032.
- Abstract
- The structure of I-HmuI, which represents the last family of homing endonucleases without a defining crystallographic structure, has been determined in complex with its DNA target. A series of diverse protein structural domains and motifs, contacting sequential stretches of nucleotide bases, are distributed along the DNA target. I-HmuI contains an N-terminal domain with a DNA-binding surface found in the I-PpoI homing endonuclease and an associated HNH/N active site found in the bacterial colicins, and a C-terminal DNA-binding domain previously observed in the I-TevI homing endonuclease. The combination and exchange of these features between protein families indicates that the genetic mobility associated with homing endonucleases extends to the level of independent structural domains. I-HmuI provides an unambiguous structural connection between the His-Cys box endonucleases and the bacterial colicins, supporting the hypothesis that these enzymes diverged from a common ancestral nuclease.
