1a0p
From Proteopedia
(Difference between revisions)
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<StructureSection load='1a0p' size='340' side='right'caption='[[1a0p]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1a0p' size='340' side='right'caption='[[1a0p]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1a0p]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A0P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A0P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1a0p]] is a 1 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=1A0P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A0P FirstGlance]. <br> |
| - | </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=1a0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0p OCA], [https://pdbe.org/1a0p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a0p RCSB], [https://www.ebi.ac.uk/pdbsum/1a0p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a0p ProSAT]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0p OCA], [https://pdbe.org/1a0p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a0p RCSB], [https://www.ebi.ac.uk/pdbsum/1a0p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a0p ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/XERD_ECOLI XERD_ECOLI] Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerC binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids at ColE1 xer (or cer) and pSC101 (or psi) sites. In the complex XerD specifically exchanges the bottom DNA strands (By similarity).<ref>PMID:7744017</ref> <ref>PMID:9268326</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1a0p ConSurf]. | </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=1a0p ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The structure of the site-specific recombinase, XerD, that functions in circular chromosome separation, has been solved at 2.5 A resolution and reveals that the protein comprises two domains. The C-terminal domain contains two conserved sequence motifs that are located in similar positions in the structures of XerD, lambda and HP1 integrases. However, the extreme C-terminal regions of the three proteins, containing the active site tyrosine, are very different. In XerD, the arrangement of active site residues supports a cis cleavage mechanism. Biochemical evidence for DNA bending is encompassed in a model that accommodates extensive biochemical and genetic data, and in which the DNA is wrapped around an alpha-helix in a manner similar to that observed for CAP complexed with DNA. | ||
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| - | Crystal structure of the site-specific recombinase, XerD.,Subramanya HS, Arciszewska LK, Baker RA, Bird LE, Sherratt DJ, Wigley DB EMBO J. 1997 Sep 1;16(17):5178-87. PMID:9311978<ref>PMID:9311978</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1a0p" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Arciszewska | + | [[Category: Arciszewska LK]] |
| - | [[Category: Baker | + | [[Category: Baker RA]] |
| - | [[Category: Bird | + | [[Category: Bird LE]] |
| - | [[Category: Sherratt | + | [[Category: Sherratt DJ]] |
| - | [[Category: Subramanya | + | [[Category: Subramanya HS]] |
| - | [[Category: Wigley | + | [[Category: Wigley DB]] |
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Current revision
SITE-SPECIFIC RECOMBINASE, XERD
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