1u3e
From Proteopedia
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DNA binding and cleavage by the HNH homing endonuclease I-HmuI
Overview
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.
About this Structure
1U3E is a Single protein structure of sequence from Enterobacteria phage sp6 with MN, SR, EDO and TRS as ligands. Full crystallographic information is available from OCA.
Reference
DNA binding and cleavage by the HNH homing endonuclease I-HmuI., Shen BW, Landthaler M, Shub DA, Stoddard BL, J Mol Biol. 2004 Sep 3;342(1):43-56. PMID:15313606
Page seeded by OCA on Wed Nov 21 03:49:18 2007
