1f44

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[[Image:1f44.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX==
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|PDB= 1f44 |SIZE=350|CAPTION= <scene name='initialview01'>1f44</scene>, resolution 2.05&Aring;
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<StructureSection load='1f44' size='340' side='right'caption='[[1f44]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
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|GENE= CRE RECOMBINASE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10711 Enterobacteria phage P21])
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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>
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}}
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f4/1f44_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1f44 ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX'''
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==See Also==
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*[[Resolvase 3D structures|Resolvase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Escherichia virus P1]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Baldwin EP]]
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1F44 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p21 Enterobacteria phage p21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F44 OCA].
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[[Category: Woods KC]]
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==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 p21]]
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[[Category: Single protein]]
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[[Category: Baldwin, E P.]]
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[[Category: Woods, K C.]]
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[[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 Thu Mar 20 11:04:07 2008''
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Current revision

CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX

PDB ID 1f44

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