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4yot
From Proteopedia
(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]] | ||
Revision as of 13:15, 15 July 2015
Crystal structure of a trimeric exonuclease PhoExo I from Pyrococcus horikoshii OT3 at 2.15A resolution
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