1U3E

DNA binding and cleavage by the HNH homing endonuclease I-HmuI

Summary for 1U3E

• Entry DOI: 10.2210/pdb1u3e/pdb
• Related: 1A73 1FSJ 1I3J 1PT3
• Descriptor: 36-MER, 5'-D(*CP*TP*TP*AP*CP*GP*TP*GP*GP*GP*AP*AP*TP*TP*GP*CP*TP*GP*AP*GP*C)-3', 5'-D(P*GP*TP*TP*AP*GP*GP*CP*TP*CP*AP*TP*TP*AP*CP*T)-3', ... (9 entities in total)
• Functional Keywords: hnh catalytic motif, helix-turn-helix dna binding domain, protein-dna complex, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Bacillus phage SPO1
• Total number of polymer chains: 4
• Total formula weight: 42874.03

Authors

Shen, B.W.,Landthaler, M.,Shub, D.A.,Stoddard, B.L. (deposition date: 2004-07-21, release date: 2004-08-31, Last modification date: 2024-04-03)

Primary citation

Shen, B.W.,Landthaler, M.,Shub, D.A.,Stoddard, B.L.
DNA Binding and Cleavage by the HNH Homing Endonuclease I-HmuI.
J.Mol.Biol., 342:43-56, 2004

PubMed 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.

PubMed: 15313606
DOI: 10.1016/j.jmb.2004.07.032

Experimental method

X-RAY DIFFRACTION (2.92 Å)