2v6e: Difference between revisions
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<StructureSection load='2v6e' size='340' side='right'caption='[[2v6e]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='2v6e' size='340' side='right'caption='[[2v6e]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2v6e]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2v6e]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_N15 Escherichia virus N15] and [https://en.wikipedia.org/wiki/Klebsiella_phage_phiKO2 Klebsiella phage phiKO2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V6E FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6e OCA], [https://pdbe.org/2v6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v6e RCSB], [https://www.ebi.ac.uk/pdbsum/2v6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v6e ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6e OCA], [https://pdbe.org/2v6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v6e RCSB], [https://www.ebi.ac.uk/pdbsum/2v6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v6e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6UAV6_9CAUD Q6UAV6_9CAUD] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia virus N15]] | ||
[[Category: Klebsiella phage phiKO2]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Aihara | [[Category: Aihara H]] | ||
[[Category: Ellenberger | [[Category: Ellenberger T]] | ||
[[Category: Huang | [[Category: Huang WM]] | ||
Latest revision as of 04:18, 28 December 2023
protelomerase TelK complexed with substrate DNAprotelomerase TelK complexed with substrate DNA
Structural highlights
FunctionPublication Abstract from PubMedThe termini of linear chromosomes are protected by specialized DNA structures known as telomeres that also facilitate the complete replication of DNA ends. The simplest type of telomere is a covalently closed DNA hairpin structure found in linear chromosomes of prokaryotes and viruses. Bidirectional replication of a chromosome with hairpin telomeres produces a catenated circular dimer that is subsequently resolved into unit-length chromosomes by a dedicated DNA cleavage-rejoining enzyme known as a hairpin telomere resolvase (protelomerase). Here we report a crystal structure of the protelomerase TelK from Klebsiella oxytoca phage varphiKO2, in complex with the palindromic target DNA. The structure shows the TelK dimer destabilizes base pairing interactions to promote the refolding of cleaved DNA ends into two hairpin ends. We propose that the hairpinning reaction is made effectively irreversible by a unique protein-induced distortion of the DNA substrate that prevents religation of the cleaved DNA substrate. An interlocked dimer of the protelomerase TelK distorts DNA structure for the formation of hairpin telomeres.,Aihara H, Huang WM, Ellenberger T Mol Cell. 2007 Sep 21;27(6):901-13. PMID:17889664[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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