4e0g

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[[Image:4e0g.jpg|left|200px]]
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==Protelomerase tela/DNA hairpin product/vanadate complex==
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<StructureSection load='4e0g' size='340' side='right' caption='[[4e0g]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4e0g]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Agrobacterium_fabrum_str._c58 Agrobacterium fabrum str. c58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E0G 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=VO4:VANADATE+ION'>VO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dwp|4dwp]], [[4e0j|4e0j]], [[4e0p|4e0p]], [[4e0y|4e0y]], [[4e0z|4e0z]], [[4e10|4e10]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">telA, Atu2523 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=176299 Agrobacterium fabrum str. C58])</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=4e0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e0g RCSB], [http://www.ebi.ac.uk/pdbsum/4e0g 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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Hairpin telomeres of bacterial linear chromosomes are generated by a DNA cutting-rejoining enzyme protelomerase. Protelomerase resolves a concatenated dimer of chromosomes as the last step of chromosome replication, converting a palindromic DNA sequence at the junctions between chromosomes into covalently closed hairpins. The mechanism by which protelomerase transforms a duplex DNA substrate into the hairpin telomeres remains largely unknown. We report here a series of crystal structures of the protelomerase TelA bound to DNA that represent distinct stages along the reaction pathway. The structures suggest that TelA converts a linear duplex substrate into hairpin turns via a transient strand-refolding intermediate that involves DNA-base flipping and wobble base-pairs. The extremely compact di-nucleotide hairpin structure of the product is fully stabilized by TelA prior to strand ligation, which drives the reaction to completion. The enzyme-catalyzed, multistep strand refolding is a novel mechanism in DNA rearrangement reactions.
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{{STRUCTURE_4e0g| PDB=4e0g | SCENE= }}
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An enzyme-catalyzed multistep DNA refolding mechanism in hairpin telomere formation.,Shi K, Huang WM, Aihara H PLoS Biol. 2013 Jan;11(1):e1001472. doi: 10.1371/journal.pbio.1001472. Epub 2013 , Jan 29. PMID:23382649<ref>PMID:23382649</ref>
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===Protelomerase tela/DNA hairpin product/vanadate complex===
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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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{{ABSTRACT_PUBMED_23382649}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[4e0g]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Agrobacterium_fabrum_str._c58 Agrobacterium fabrum str. c58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E0G OCA].
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</StructureSection>
[[Category: Agrobacterium fabrum str. c58]]
[[Category: Agrobacterium fabrum str. c58]]
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[[Category: Aihara, H.]]
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[[Category: Aihara, H]]
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[[Category: Shi, K.]]
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[[Category: Shi, K]]
[[Category: Dna binding protein-dna complex]]
[[Category: Dna binding protein-dna complex]]
[[Category: Dna hairpin]]
[[Category: Dna hairpin]]
[[Category: Dna pairpin]]
[[Category: Dna pairpin]]
[[Category: Protelemorase]]
[[Category: Protelemorase]]

Revision as of 17:24, 9 December 2014

Protelomerase tela/DNA hairpin product/vanadate complex

4e0g, resolution 2.20Å

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