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New page: left|200px<br /><applet load="1zr2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zr2, resolution 3.90Å" /> '''Structure of a Synap... |
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== | ==Structure of a Synaptic gamma-delta Resolvase Tetramer Covalently Linked to two Cleaved DNAs== | ||
The structure of a synaptic intermediate of the site-specific recombinase | <StructureSection load='1zr2' size='340' side='right'caption='[[1zr2]], [[Resolution|resolution]] 3.90Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1zr2]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZR2 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]] 3.9Å</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=1zr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zr2 OCA], [https://pdbe.org/1zr2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zr2 RCSB], [https://www.ebi.ac.uk/pdbsum/1zr2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zr2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TNR1_ECOLI TNR1_ECOLI] This protein catalyzes the site-specific recombination of the transposon and also regulates its frequency of transposition. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zr/1zr2_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zr2 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structure of a synaptic intermediate of the site-specific recombinase gammadelta resolvase covalently linked through Ser10 to two cleaved duplex DNAs has been determined at 3.4 angstrom resolution. This resolvase, activated for recombination by mutations, forms a tetramer whose structure is substantially changed from that of a presynaptic complex between dimeric resolvase and the cleavage site DNA. Because the two cleaved DNA duplexes that are to be recombined lie on opposite sides of the core tetramer, large movements of both protein and DNA are required to achieve strand exchange. The two dimers linked to the DNAs that are to be recombined are held together by a flat interface. This may allow a 180 degrees rotation of one dimer relative to the other in order to reposition the DNA duplexes for strand exchange. | |||
Structure of a synaptic gammadelta resolvase tetramer covalently linked to two cleaved DNAs.,Li W, Kamtekar S, Xiong Y, Sarkis GJ, Grindley ND, Steitz TA Science. 2005 Aug 19;309(5738):1210-5. Epub 2005 Jun 30. PMID:15994378<ref>PMID:15994378</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1zr2" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Resolvase 3D structures|Resolvase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Grindley | [[Category: Grindley ND]] | ||
[[Category: Kamtekar | [[Category: Kamtekar S]] | ||
[[Category: Li | [[Category: Li W]] | ||
[[Category: Sarkis | [[Category: Sarkis GJ]] | ||
[[Category: Steitz | [[Category: Steitz TA]] | ||
[[Category: Xiong | [[Category: Xiong Y]] | ||
Latest revision as of 08:04, 17 October 2024
Structure of a Synaptic gamma-delta Resolvase Tetramer Covalently Linked to two Cleaved DNAsStructure of a Synaptic gamma-delta Resolvase Tetramer Covalently Linked to two Cleaved DNAs
Structural highlights
FunctionTNR1_ECOLI This protein catalyzes the site-specific recombination of the transposon and also regulates its frequency of transposition. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of a synaptic intermediate of the site-specific recombinase gammadelta resolvase covalently linked through Ser10 to two cleaved duplex DNAs has been determined at 3.4 angstrom resolution. This resolvase, activated for recombination by mutations, forms a tetramer whose structure is substantially changed from that of a presynaptic complex between dimeric resolvase and the cleavage site DNA. Because the two cleaved DNA duplexes that are to be recombined lie on opposite sides of the core tetramer, large movements of both protein and DNA are required to achieve strand exchange. The two dimers linked to the DNAs that are to be recombined are held together by a flat interface. This may allow a 180 degrees rotation of one dimer relative to the other in order to reposition the DNA duplexes for strand exchange. Structure of a synaptic gammadelta resolvase tetramer covalently linked to two cleaved DNAs.,Li W, Kamtekar S, Xiong Y, Sarkis GJ, Grindley ND, Steitz TA Science. 2005 Aug 19;309(5738):1210-5. Epub 2005 Jun 30. PMID:15994378[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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