5hxy
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of XerA recombinase== | |
| + | <StructureSection load='5hxy' size='340' side='right' caption='[[5hxy]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5hxy]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HXY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HXY FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5hxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hxy OCA], [http://pdbe.org/5hxy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hxy RCSB], [http://www.ebi.ac.uk/pdbsum/5hxy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hxy ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/Q9HIM5_THEAC Q9HIM5_THEAC]] Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules.[HAMAP-Rule:MF_02055] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Site-specific Xer recombination plays a pivotal role in reshuffling genetic information. Here, we report the 2.5 A crystal structure of XerA from the archaean Thermoplasma acidophilum. Crystallographic data reveal a uniquely open conformational state, resulting in a C-shaped clamp with an angle of ~ 48 degrees and a distance of 57 A between the core-binding and the catalytic domains. The catalytic nucleophile, Tyr264, is positioned in cis-cleavage mode by XerA's C-term tail that interacts with the CAT domain of a neighboring monomer without DNA substrate. Structural comparisons of tyrosine recombinases elucidate the dynamics of Xer recombinase. | ||
| - | + | Crystal structure of Thermoplasma acidophilum XerA recombinase shows large C-shape clamp conformation and cis-cleavage mode for nucleophilic tyrosine.,Jo CH, Kim J, Han AR, Park SY, Hwang KY, Nam KH FEBS Lett. 2016 Mar;590(6):848-56. doi: 10.1002/1873-3468.12109. Epub 2016 Mar 4. PMID:26919387<ref>PMID:26919387</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Hwang, K | + | <div class="pdbe-citations 5hxy" style="background-color:#fffaf0;"></div> |
| - | [[Category: Nam, K | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Hwang, K Y]] | ||
| + | [[Category: Nam, K H]] | ||
| + | [[Category: Recombinase]] | ||
| + | [[Category: Recombination]] | ||
| + | [[Category: Xera]] | ||
Revision as of 17:58, 1 February 2017
Crystal structure of XerA recombinase
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Categories: Hwang, K Y | Nam, K H | Recombinase | Recombination | Xera
