5o6i
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structures and dynamics of mesophilic variants from the homing endonuclease I-DmoI== | |
| + | <StructureSection load='5o6i' size='340' side='right' caption='[[5o6i]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5o6i]] is a 9 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O6I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O6I FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=5o6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o6i OCA], [http://pdbe.org/5o6i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o6i RCSB], [http://www.ebi.ac.uk/pdbsum/5o6i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o6i ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | I-DmoI, from the hyperthermophilic archaeon Desulfurococcus mobilis, belongs to the LAGLIDADG homing endonuclease protein family. Its members are highly specific enzymes capable of recognizing long DNA target sequences, thus providing potential tools for genome manipulation. Working towards this particular application, many efforts have been made to generate mesophilic variants of I-DmoI that function at lower temperatures than the wild-type. Here, we report a structural and computational analysis of two I-DmoI mesophilic mutants. Despite very limited structural variations between the crystal structures of these variants and the wild-type, a different dynamical behaviour near the cleavage sites is observed. In particular, both the dynamics of the water molecules and the protein perturbation effect on the cleavage site correlate well with the changes observed in the experimental enzymatic activity. | ||
| - | + | Structure and dynamics of mesophilic variants from the homing endonuclease I-DmoI.,Alba J, Marcaida MJ, Prieto J, Montoya G, Molina R, D'Abramo M J Comput Aided Mol Des. 2017 Nov 25. pii: 10.1007/s10822-017-0087-5. doi:, 10.1007/s10822-017-0087-5. PMID:29177929<ref>PMID:29177929</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5o6i" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Marcaida, M J]] | ||
[[Category: Molina, R]] | [[Category: Molina, R]] | ||
| - | [[Category: | + | [[Category: Desulfurococcus mobili]] |
| + | [[Category: Dna binding protein]] | ||
Revision as of 07:11, 6 December 2017
Structures and dynamics of mesophilic variants from the homing endonuclease I-DmoI
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