1u3e

<StructureSection load='1u3e' size='340' side='right' caption='[[1u3e]], [[Resolution|resolution]] 2.92&Aring;' scene=''>

<table><tr><td colspan='2'>[[1u3e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpsp1 Bpsp1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U3E FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bacteriophage SP01 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10685 BPSP1])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u3e OCA], [http://pdbe.org/1u3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u3e RCSB], [http://www.ebi.ac.uk/pdbsum/1u3e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u3e ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15313606</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1u3e" style="background-color:#fffaf0;"></div>

*[[Endonuclease|Endonuclease]]

[[Category: Bpsp1]]

[[Category: Landthaler, M]]

[[Category: Shen, B W]]

[[Category: Shub, D A]]

[[Category: Stoddard, B L]]

[[Category: Dna binding protein-dna complex]]

[[Category: Protein-dna complex]]