4e10: Difference between revisions
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The | ==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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4E10 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.506Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BRU:5-BROMO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>BRU</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</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=4e10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e10 OCA], [https://pdbe.org/4e10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e10 RCSB], [https://www.ebi.ac.uk/pdbsum/4e10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e10 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q7CWV1_AGRFC Q7CWV1_AGRFC] | |||
<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> | |||
<div class="pdbe-citations 4e10" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Agrobacterium fabrum str. C58]] | |||
[[Category: Large Structures]] | |||
[[Category: Aihara H]] | |||
[[Category: Shi K]] | |||
Latest revision as of 11:18, 9 October 2024
Protelomerase tela Y201A covalently complexed with substrate DNAProtelomerase tela Y201A covalently complexed with substrate DNA
Structural highlights
FunctionPublication Abstract from PubMedHairpin 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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