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| [[Image:1f44.gif|left|200px]]
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| <!-- | | ==CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX== |
| The line below this paragraph, containing "STRUCTURE_1f44", creates the "Structure Box" on the page.
| | <StructureSection load='1f44' size='340' side='right'caption='[[1f44]], [[Resolution|resolution]] 2.05Å' scene=''> |
| You may change the PDB parameter (which sets the PDB file loaded into the applet)
| | == Structural highlights == |
| or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| | <table><tr><td colspan='2'>[[1f44]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_P1 Escherichia virus P1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F44 FirstGlance]. <br> |
| or leave the SCENE parameter empty for the default display.
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</td></tr> |
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f44 OCA], [https://pdbe.org/1f44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f44 RCSB], [https://www.ebi.ac.uk/pdbsum/1f44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f44 ProSAT]</span></td></tr> |
| {{STRUCTURE_1f44| PDB=1f44 | SCENE= }}
| | </table> |
| | == Function == |
| | [https://www.uniprot.org/uniprot/RECR_BPP1 RECR_BPP1] Catalyzes site-specific recombination between two 34-base-pair LOXP sites. Its role is to maintain the phage genome as a monomeric unit-copy plasmid in the lysogenic state. |
| | == 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/f4/1f44_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1f44 ConSurf]. |
| | <div style="clear:both"></div> |
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| '''CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX'''
| | ==See Also== |
| | | *[[Resolvase 3D structures|Resolvase 3D structures]] |
| | | __TOC__ |
| ==Overview==
| | </StructureSection> |
| The crystal structure of a novel Cre-Lox synapse was solved using phases from multiple isomorphous replacement and anomalous scattering, and refined to 2.05 A resolution. In this complex, a symmetric protein trimer is bound to a Y-shaped three-way DNA junction, a marked departure from the pseudo-4-fold symmetrical tetramer associated with Cre-mediated LoxP recombination. The three-way DNA junction was accommodated by a simple kink without significant distortion of the adjoining DNA duplexes. Although the mean angle between DNA arms in the Y and X structures was similar, adjacent Cre trimer subunits rotated 29 degrees relative to those in the tetramers. This rotation was accommodated at the protein-protein and DNA-DNA interfaces by interactions that are "quasi-equivalent" to those in the tetramer, analogous to packing differences of chemically identical viral subunits at non-equivalent positions in icosahedral capsids. This structural quasi-equivalence extends to function as Cre can bind to, cleave and perform strand transfer with a three-way Lox substrate. The structure explains the dual recognition of three and four-way junctions by site-specific recombinases as being due to shared structural features between the differently branched substrates and plasticity of the protein-protein interfaces. To our knowledge, this is the first direct demonstration of quasi-equivalence in both the assembly and function of an oligomeric enzyme.
| | [[Category: Escherichia virus P1]] |
| | | [[Category: Large Structures]] |
| ==About this Structure== | | [[Category: Baldwin EP]] |
| 1F44 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p1 Enterobacteria phage p1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F44 OCA].
| | [[Category: Woods KC]] |
| | |
| ==Reference==
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| Quasi-equivalence in site-specific recombinase structure and function: crystal structure and activity of trimeric Cre recombinase bound to a three-way Lox DNA junction., Woods KC, Martin SS, Chu VC, Baldwin EP, J Mol Biol. 2001 Oct 12;313(1):49-69. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11601846 11601846]
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| [[Category: Enterobacteria phage p1]] | |
| [[Category: Single protein]] | |
| [[Category: Baldwin, E P.]] | |
| [[Category: Woods, K C.]] | |
| [[Category: Branched dna]]
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| [[Category: Hydrolase]]
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| [[Category: Ligase/dna]]
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| [[Category: Protein-dna complex]]
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| [[Category: Recombination]]
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| [[Category: Site-specific recombinase]]
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| [[Category: Three-way junction]]
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| [[Category: Trimeric]]
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| [[Category: Y-junction]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:52:24 2008''
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