5jk0: Difference between revisions
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<StructureSection load='5jk0' size='340' side='right'caption='[[5jk0]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='5jk0' size='340' side='right'caption='[[5jk0]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5jk0]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5jk0]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JK0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JK0 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=5jk0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jk0 OCA], [https://pdbe.org/5jk0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jk0 RCSB], [https://www.ebi.ac.uk/pdbsum/5jk0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jk0 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/XERH_HELPY XERH_HELPY] Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Involved in chromosome segregation. May contribute to chromosome decatenation.<ref>PMID:22511919</ref> | ||
<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: Helicobacter pylori 26695]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Barabas | [[Category: Barabas O]] | ||
[[Category: Bebel | [[Category: Bebel A]] | ||
Latest revision as of 21:56, 20 September 2023
Crystal structure of XerH site-specific recombinase bound to difH substrate: pre-cleavage complexCrystal structure of XerH site-specific recombinase bound to difH substrate: pre-cleavage complex
Structural highlights
FunctionXERH_HELPY Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Involved in chromosome segregation. May contribute to chromosome decatenation.[1] Publication Abstract from PubMedBacterial Xer site-specific recombinases play an essential genome maintenance role by unlinking chromosome multimers, but their mechanism of action has remained structurally uncharacterized. Here, we present two high-resolution structures of Helicobacter pylori XerH with its recombination site DNA difH, representing pre-cleavage and post-cleavage synaptic intermediates in the recombination pathway. The structures reveal that activation of DNA strand cleavage and rejoining involves large conformational changes and DNA bending, suggesting how interaction with the cell division protein FtsK may license recombination at the septum. Together with biochemical and in vivo analysis, our structures also reveal how a small sequence asymmetry in difH defines protein conformation in the synaptic complex and orchestrates the order of DNA strand exchanges. Our results provide insights into the catalytic mechanism of Xer recombination and a model for regulation of recombination activity during cell division. Structural snapshots of Xer recombination reveal activation by synaptic complex remodeling and DNA bending.,Bebel A, Karaca E, Kumar B, Stark WM, Barabas O Elife. 2016 Dec 23;5. pii: e19706. doi: 10.7554/eLife.19706. PMID:28009253[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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