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| | <StructureSection load='5hxy' size='340' side='right'caption='[[5hxy]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='5hxy' size='340' side='right'caption='[[5hxy]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hxy]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Theac Theac]. 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> | + | <table><tr><td colspan='2'>[[5hxy]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum_DSM_1728 Thermoplasma acidophilum DSM 1728]. 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 [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">xerA, Ta1314 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273075 THEAC])</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=5hxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hxy OCA], [https://pdbe.org/5hxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hxy RCSB], [https://www.ebi.ac.uk/pdbsum/5hxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hxy ProSAT]</span></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> | | </table> |
| | == Function == | | == 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] | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Theac]] | + | [[Category: Thermoplasma acidophilum DSM 1728]] |
| - | [[Category: Hwang, K Y]] | + | [[Category: Hwang KY]] |
| - | [[Category: Nam, K H]] | + | [[Category: Nam KH]] |
| - | [[Category: Recombinase]]
| + | |
| - | [[Category: Recombination]]
| + | |
| - | [[Category: Xera]]
| + | |
| Structural highlights
Function
Q9HIM5_THEAC Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules.[HAMAP-Rule:MF_02055]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jo CH, Kim J, Han AR, Park SY, Hwang KY, Nam KH. Crystal structure of Thermoplasma acidophilum XerA recombinase shows large C-shape clamp conformation and cis-cleavage mode for nucleophilic tyrosine. FEBS Lett. 2016 Mar;590(6):848-56. doi: 10.1002/1873-3468.12109. Epub 2016 Mar 4. PMID:26919387 doi:http://dx.doi.org/10.1002/1873-3468.12109
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