1drg: Difference between revisions

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-[[Image:1drg.gif|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX==
-|PDB= 1drg |SIZE=350|CAPTION= <scene name='initialview01'>1drg</scene>, resolution 2.55&Aring;
+<StructureSection load='1drg' size='340' side='right'caption='[[1drg]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[1drg]] 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=1DRG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DRG FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
-|GENE=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1drg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1drg OCA], [https://pdbe.org/1drg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1drg RCSB], [https://www.ebi.ac.uk/pdbsum/1drg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1drg ProSAT]</span></td></tr>
-}}
+</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/dr/1drg_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=1drg ConSurf].
+<div style="clear:both"></div>
-'''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]]
-DRG 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=1DRG OCA].
+[[Category: Woods KC]]
-==Reference==
-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]
-[[Category: Enterobacteria phage p21]]
-[[Category: Single protein]]
-[[Category: Baldwin, E P.]]
-[[Category: Woods, K C.]]
-[[Category: branched dna]]
-[[Category: protein-dna complex]]
-[[Category: recombination]]
-[[Category: site-specific recombinase]]
-[[Category: three- way junction]]
-[[Category: trimeric]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:43:07 2008''