4yoy

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'''Unreleased structure'''
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==Crystal structure of a trimeric exonuclease PhoExo I from Pyrococcus horikoshii OT3 in complex with poly-dT and Mg2+ ion==
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<StructureSection load='4yoy' size='340' side='right' caption='[[4yoy]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4yoy]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YOY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YOY 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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yor|4yor]], [[4yot|4yot]], [[4you|4you]], [[4yov|4yov]], [[4yow|4yow]], [[4yox|4yox]]</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=4yoy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yoy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4yoy RCSB], [http://www.ebi.ac.uk/pdbsum/4yoy PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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The entry 4yoy is ON HOLD until Paper Publication
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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>
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Authors: Miyazono, K., Ito, T., Tanokura, M.
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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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Description:
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Ito, T]]
[[Category: Ito, T]]
[[Category: Miyazono, K]]
[[Category: Miyazono, K]]
[[Category: Tanokura, M]]
[[Category: Tanokura, M]]
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[[Category: Exonuclease]]
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[[Category: Hydrolase-dna complex]]

Revision as of 13:24, 15 July 2015

Crystal structure of a trimeric exonuclease PhoExo I from Pyrococcus horikoshii OT3 in complex with poly-dT and Mg2+ ion

4yoy, resolution 1.95Å

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