1i3j

<StructureSection load='1i3j' size='340' side='right' caption='[[1i3j]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[1i3j]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I3J FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1i3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i3j OCA], [http://pdbe.org/1i3j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i3j RCSB], [http://www.ebi.ac.uk/pdbsum/1i3j PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/TEV1_BPT4 TEV1_BPT4]] This endonuclease is specific to the thymidylate synthase (td) gene splice junction and is involved in intron homing.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i3/1i3j_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

I-TevI is a site-specific, sequence-tolerant intron endonuclease. The crystal structure of the DNA-binding domain of I-TevI complexed with the 20 bp primary binding region of its DNA target reveals an unusually extended structure composed of three subdomains: a Zn finger, an elongated segment containing a minor groove-binding alpha-helix, and a helix-turn-helix. The protein wraps around the DNA, mostly following the minor groove, contacting the phosphate backbone along the full length of the duplex. Surprisingly, while the minor groove-binding helix and the helix-turn- helix subdomain make hydrophobic contacts, the few base-specific hydrogen bonds occur in segments that lack secondary structure and flank the intron insertion site. The multiple base-specific interactions over a long segment of the substrate are consistent with the observed high site specificity in spite of sequence tolerance, while the modular composition of the domain is pertinent to the evolution of homing endonucleases.

Intertwined structure of the DNA-binding domain of intron endonuclease I-TevI with its substrate.,Van Roey P, Waddling CA, Fox KM, Belfort M, Derbyshire V EMBO J. 2001 Jul 16;20(14):3631-7. PMID:11447104<ref>PMID:11447104</ref>

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

</div>

<div class="pdbe-citations 1i3j" style="background-color:#fffaf0;"></div>

*[[Endonuclease|Endonuclease]]

[[Category: Bpt4]]

[[Category: Belfort, M]]

[[Category: Derbyshire, V]]

[[Category: Fox, K M]]

[[Category: Roey, P Van]]

[[Category: Waddling, C A]]

[[Category: Zn-finger]]