4yot: Difference between revisions
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''' | ==Crystal structure of a trimeric exonuclease PhoExo I from Pyrococcus horikoshii OT3 at 2.15A resolution== | ||
<StructureSection load='4yot' size='340' side='right' caption='[[4yot]], [[Resolution|resolution]] 2.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4yot]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YOT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YOT FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yor|4yor]], [[4you|4you]], [[4yov|4yov]], [[4yow|4yow]], [[4yox|4yox]], [[4yoy|4yoy]]</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=4yot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yot OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4yot RCSB], [http://www.ebi.ac.uk/pdbsum/4yot PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nucleases play important roles in nucleic acid processes, such as replication, repair and recombination. Recently, we identified a novel single-strand specific 3'-5' exonuclease, PfuExo I, from the hyperthermophilic archaeon Pyrococcus furiosus, which may be involved in the Thermococcales-specific DNA repair system. PfuExo I forms a trimer and cleaves single-stranded DNA at every two nucleotides. Here, we report the structural basis for the cleavage mechanism of this novel exonuclease family. A structural analysis of PhoExo I, the homologous enzyme from P. horikoshii OT3, showed that PhoExo I utilizes an RNase H-like active site and possesses a 3'-OH recognition site approximately 9 A away from the active site, which enables cleavage at every two nucleotides. Analyses of the heterotrimeric and monomeric PhoExo I activities showed that trimerization is indispensable for its processive cleavage mechanism, but only one active site of the trimer is required. | |||
Structural basis for substrate recognition and processive cleavage mechanisms of the trimeric exonuclease PhoExo I.,Miyazono KI, Ishino S, Tsutsumi K, Ito T, Ishino Y, Tanokura M Nucleic Acids Res. 2015 Jul 2. pii: gkv654. PMID:26138487<ref>PMID:26138487</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Miyazono, K]] | [[Category: Miyazono, K]] | ||
[[Category: Tanokura, M]] | [[Category: Tanokura, M]] | ||
[[Category: Tsutsumi, K]] | [[Category: Tsutsumi, K]] | ||
[[Category: Exonuclease]] | |||