1m5x

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<StructureSection load='1m5x' size='340' side='right'caption='[[1m5x]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='1m5x' size='340' side='right'caption='[[1m5x]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1m5x]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Monsk Monsk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M5X FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1m5x]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Monomastix_sp._OKE-1 Monomastix sp. OKE-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M5X 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=CA:CALCIUM+ION'>CA</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]] 2.25&#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=1m5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m5x OCA], [http://pdbe.org/1m5x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m5x RCSB], [http://www.ebi.ac.uk/pdbsum/1m5x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m5x 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=CA:CALCIUM+ION'>CA</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=1m5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m5x OCA], [https://pdbe.org/1m5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m5x RCSB], [https://www.ebi.ac.uk/pdbsum/1m5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m5x ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/C0JWR6_MONSK C0JWR6_MONSK]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1m5x ConSurf].
</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=1m5x ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Homing endonucleases are highly specific catalysts of DNA strand breaks that induce the transposition of mobile intervening sequences containing the endonuclease open reading frame. These enzymes recognize long DNA targets while tolerating individual sequence polymorphisms within those sites. Sequences of the homing endonucleases themselves diversify to a great extent after founding intron invasion events, generating highly divergent enzymes that recognize similar target sequences. Here, we visualize the mechanism of flexible DNA recognition and the pattern of structural divergence displayed by two homing endonuclease isoschizomers. We determined structures of I-CreI bound to two DNA target sites that differ at eight of 22 base-pairs, and the structure of an isoschizomer, I-MsoI, bound to a nearly identical DNA target site. This study illustrates several principles governing promiscuous base-pair recognition by DNA-binding proteins, and demonstrates that the isoschizomers display strikingly different protein/DNA contacts. The structures allow us to determine the information content at individual positions in the binding site as a function of the distribution of direct and water-mediated contacts to nucleotide bases, and provide an evolutionary snapshot of endonucleases at an early stage of divergence in their target specificity.
 
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Flexible DNA target site recognition by divergent homing endonuclease isoschizomers I-CreI and I-MsoI.,Chevalier B, Turmel M, Lemieux C, Monnat RJ Jr, Stoddard BL J Mol Biol. 2003 May 30;329(2):253-69. PMID:12758074<ref>PMID:12758074</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 1m5x" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Monsk]]
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[[Category: Monomastix sp. OKE-1]]
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[[Category: Chevalier, B]]
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[[Category: Chevalier B]]
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[[Category: Lemieux, C]]
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[[Category: Lemieux C]]
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[[Category: Monnat, R J]]
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[[Category: Monnat RJ]]
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[[Category: Stoddard, B L]]
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[[Category: Stoddard BL]]
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[[Category: Turmel, M]]
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[[Category: Turmel M]]
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[[Category: Hydrolase-dna complex]]
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[[Category: Laglidadg]]
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Current revision

Crystal structure of the homing endonuclease I-MsoI bound to its DNA substrate

PDB ID 1m5x

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