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1ipp

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==HOMING ENDONUCLEASE/DNA COMPLEX==
==HOMING ENDONUCLEASE/DNA COMPLEX==
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<StructureSection load='1ipp' size='340' side='right' caption='[[1ipp]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='1ipp' size='340' side='right'caption='[[1ipp]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1ipp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Phypo Phypo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IPP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IPP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1ipp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Physarum_polycephalum Physarum polycephalum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IPP FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<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=1ipp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ipp OCA], [http://pdbe.org/1ipp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ipp RCSB], [http://www.ebi.ac.uk/pdbsum/1ipp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ipp ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ipp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ipp OCA], [https://pdbe.org/1ipp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ipp RCSB], [https://www.ebi.ac.uk/pdbsum/1ipp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ipp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PPO1_PHYPO PPO1_PHYPO]] Mediates the homing of a group I intron in the ribosomal DNA. Makes a four-base staggered cut in its ribosomal DNA target sequence.
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[https://www.uniprot.org/uniprot/PPO1_PHYPO PPO1_PHYPO] Mediates the homing of a group I intron in the ribosomal DNA. Makes a four-base staggered cut in its ribosomal DNA target sequence.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Homing endonucleases are a diverse collection of proteins that are encoded by genes with mobile, self-splicing introns. They have also been identified in self-splicing inteins (protein introns). These enzymes promote the movement of the DNA sequences that encode them from one chromosome location to another; they do this by making a site-specific double-strand break at a target site in an allele that lacks the corresponding mobile intron. The target sites recognized by these small endonucleases are generally long (14-44 base pairs). Four families of homing endonucleases have been identified, including the LAGLIDADG, the His-Cys box, the GIY-YIG and the H-N-H endonucleases. The first identified His-Cys box homing endonuclease was I-PpoI from the slime mould Physarum polycephalum. Its gene resides in one of only a few nuclear introns known to exhibit genetic mobility. Here we report the structure of the I-PpoI homing endonuclease bound to homing-site DNA determined to 1.8 A resolution. I-PpoI displays an elongated fold of dimensions 25 x 35 x 80 A, with mixed alpha/beta topology. Each I-PpoI monomer contains three antiparallel beta-sheets flanked by two long alpha-helices and a long carboxy-terminal tail, and is stabilized by two bound zinc ions 15 A apart. The enzyme possesses a new zinc-bound fold and endonuclease active site. The structure has been determined in both uncleaved substrate and cleaved product complexes.
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DNA binding and cleavage by the nuclear intron-encoded homing endonuclease I-PpoI.,Flick KE, Jurica MS, Monnat RJ Jr, Stoddard BL Nature. 1998 Jul 2;394(6688):96-101. PMID:9665136<ref>PMID:9665136</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ipp" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Endonuclease|Endonuclease]]
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*[[Endonuclease 3D structures|Endonuclease 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Phypo]]
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[[Category: Large Structures]]
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[[Category: Flick, K E]]
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[[Category: Physarum polycephalum]]
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[[Category: Jurica, M S]]
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[[Category: Flick KE]]
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[[Category: Monnat, R J]]
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[[Category: Jurica MS]]
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[[Category: Stoddard, B L]]
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[[Category: Monnat Jr RJ]]
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[[Category: Dna binding]]
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[[Category: Stoddard BL]]
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[[Category: Homing endonuclease]]
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[[Category: Intron]]
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[[Category: Protein folding]]
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[[Category: Transcription-dna complex]]
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[[Category: Transcription/dna]]
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[[Category: Zinc]]
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Current revision

HOMING ENDONUCLEASE/DNA COMPLEX

PDB ID 1ipp

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