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[[Image:1bp7.gif|left|200px]]
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{{STRUCTURE_1bp7|  PDB=1bp7  |  SCENE=  }}
'''GROUP I MOBILE INTRON ENDONUCLEASE I-CREI COMPLEXED WITH HOMING SITE DNA'''


==GROUP I MOBILE INTRON ENDONUCLEASE I-CREI COMPLEXED WITH HOMING SITE DNA==
<StructureSection load='1bp7' size='340' side='right'caption='[[1bp7]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bp7]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BP7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bp7 OCA], [https://pdbe.org/1bp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bp7 RCSB], [https://www.ebi.ac.uk/pdbsum/1bp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bp7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DNE1_CHLRE DNE1_CHLRE] Endonuclease involved in group I intron homing. Recognizes and cleaves a 19-24 bp palindromic DNA site.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bp/1bp7_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/main_output.php?pdb_ID=1bp7 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of the LAGLIDADG intron-encoded homing endonuclease I-CreI bound to homing site DNA has been determined. The interface is formed by an extended, concave beta sheet from each enzyme monomer that contacts each DNA half-site, resulting in direct side-chain contacts to 18 of the 24 base pairs across the full-length homing site. The structure indicates that I-CreI is optimized to its role in genetic transposition by exhibiting long site-recognition while being able to cleave many closely related target sequences. DNA cleavage is mediated by a compact pair of active sites in the I-CreI homodimer, each of which contains a separate bound divalent cation.


==Overview==
DNA recognition and cleavage by the LAGLIDADG homing endonuclease I-CreI.,Jurica MS, Monnat RJ Jr, Stoddard BL Mol Cell. 1998 Oct;2(4):469-76. PMID:9809068<ref>PMID:9809068</ref>
The structure of the LAGLIDADG intron-encoded homing endonuclease I-CreI bound to homing site DNA has been determined. The interface is formed by an extended, concave beta sheet from each enzyme monomer that contacts each DNA half-site, resulting in direct side-chain contacts to 18 of the 24 base pairs across the full-length homing site. The structure indicates that I-CreI is optimized to its role in genetic transposition by exhibiting long site-recognition while being able to cleave many closely related target sequences. DNA cleavage is mediated by a compact pair of active sites in the I-CreI homodimer, each of which contains a separate bound divalent cation.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1BP7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BP7 OCA].
</div>
<div class="pdbe-citations 1bp7" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
DNA recognition and cleavage by the LAGLIDADG homing endonuclease I-CreI., Jurica MS, Monnat RJ Jr, Stoddard BL, Mol Cell. 1998 Oct;2(4):469-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9809068 9809068]
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chlamydomonas reinhardtii]]
[[Category: Chlamydomonas reinhardtii]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Junior, R J.Monnat.]]
[[Category: Jurica MS]]
[[Category: Jurica, M S.]]
[[Category: Monnat Junior RJ]]
[[Category: Stoddard, B L.]]
[[Category: Stoddard BL]]
[[Category: Chloroplast dna]]
[[Category: Dna complex]]
[[Category: Endonuclease]]
[[Category: Group i mobile intron]]
[[Category: Intron homing]]
[[Category: Laglidadg motif]]
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Retrieved from "https://proteopedia.org/1bp7"