4e10: Difference between revisions
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[[ | ==Protelomerase tela Y201A covalently complexed with substrate DNA== | ||
<StructureSection load='4e10' size='340' side='right' caption='[[4e10]], [[Resolution|resolution]] 2.51Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4e10]] 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=4E10 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E10 FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BRU:5-BROMO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>BRU</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dwp|4dwp]], [[4e0g|4e0g]], [[4e0j|4e0j]], [[4e0p|4e0p]], [[4e0y|4e0y]], [[4e0z|4e0z]]</td></tr> | |||
<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> | |||
<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=4e10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e10 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e10 RCSB], [http://www.ebi.ac.uk/pdbsum/4e10 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Agrobacterium fabrum str. c58]] | [[Category: Agrobacterium fabrum str. c58]] | ||
[[Category: Aihara, H | [[Category: Aihara, H]] | ||
[[Category: Shi, K | [[Category: Shi, K]] | ||
[[Category: Dna binding protein-dna complex]] | [[Category: Dna binding protein-dna complex]] | ||
[[Category: Protelemorase]] | [[Category: Protelemorase]] | ||
