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1mow

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[[Image:1mow.gif|left|200px]]
 
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{{Structure
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==E-DreI==
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|PDB= 1mow |SIZE=350|CAPTION= <scene name='initialview01'>1mow</scene>, resolution 2.40&Aring;
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<StructureSection load='1mow' size='340' side='right'caption='[[1mow]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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<table><tr><td colspan='2'>[[1mow]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii] and [https://en.wikipedia.org/wiki/Desulfurococcus_mucosus Desulfurococcus mucosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MOW FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.4&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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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=1mow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mow OCA], [https://pdbe.org/1mow PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mow RCSB], [https://www.ebi.ac.uk/pdbsum/1mow PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mow ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DMO1_DESMO DMO1_DESMO] Endonuclease involved in intron homing. Recognizes a recognizes up to 20 bp of DNA in the 23S rRNA gene intron. It has a slow turnover rate and cuts the coding strand with a slight preference over the non-coding strand.[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/1mow_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1mow ConSurf].
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<div style="clear:both"></div>
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'''E-DreI'''
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==See Also==
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*[[Endonuclease 3D structures|Endonuclease 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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We have generated an artificial highly specific endonuclease by fusing domains of homing endonucleases I-DmoI and I-CreI and creating a new 1400 A(2) protein interface between these domains. Protein engineering was accomplished by combining computational redesign and an in vivo protein-folding screen. The resulting enzyme, E-DreI (Engineered I-DmoI/I-CreI), binds a long chimeric DNA target site with nanomolar affinity, cleaving it precisely at a rate equivalent to its natural parents. The structure of an E-DreI/DNA complex demonstrates the accuracy of the protein interface redesign algorithm and reveals how catalytic function is maintained during the creation of the new endonuclease. These results indicate that it may be possible to generate novel highly specific DNA binding proteins from homing endonucleases.
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[[Category: Chlamydomonas reinhardtii]]
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[[Category: Desulfurococcus mucosus]]
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==About this Structure==
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[[Category: Large Structures]]
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1MOW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Desulfurococcus_mobilis_and_chlamydomonas_reinhardtii Desulfurococcus mobilis and chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOW OCA].
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[[Category: Baker D]]
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[[Category: Chadsey MS]]
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==Reference==
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[[Category: Chevalier BS]]
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Design, activity, and structure of a highly specific artificial endonuclease., Chevalier BS, Kortemme T, Chadsey MS, Baker D, Monnat RJ, Stoddard BL, Mol Cell. 2002 Oct;10(4):895-905. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12419232 12419232]
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[[Category: Kortemme T]]
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[[Category: Desulfurococcus mobilis and chlamydomonas reinhardtii]]
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[[Category: Monnat Jr RJ]]
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[[Category: Single protein]]
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[[Category: Stoddard BL]]
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[[Category: Baker, D.]]
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[[Category: Chadsey, M S.]]
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[[Category: Chevalier, B S.]]
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[[Category: Jr., R J.Monnat.]]
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[[Category: Kortemme, T.]]
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[[Category: Stoddard, B L.]]
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[[Category: GOL]]
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[[Category: MG]]
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[[Category: SO4]]
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[[Category: design]]
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[[Category: endonuclease]]
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[[Category: engineering]]
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[[Category: homing]]
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[[Category: laglidadg]]
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[[Category: structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:46:13 2008''
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Current revision

E-DreI

PDB ID 1mow

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