1f44: Difference between revisions

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<StructureSection load='1f44' size='340' side='right'caption='[[1f44]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
<StructureSection load='1f44' size='340' side='right'caption='[[1f44]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1f44]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpp1 Bpp1]. 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>
<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>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1drg|1drg]]</div></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]] 2.05&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRE RECOMBINASE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10678 BPP1])</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=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>
<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>
</table>
</table>
== Function ==
== 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.  
[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 ==
== 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=1f44 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=1f44 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:11601846<ref>PMID:11601846</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1f44" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Resolvase 3D structures|Resolvase 3D structures]]
*[[Resolvase 3D structures|Resolvase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bpp1]]
[[Category: Escherichia virus P1]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Baldwin, E P]]
[[Category: Baldwin EP]]
[[Category: Woods, K C]]
[[Category: Woods KC]]
[[Category: Branched dna]]
[[Category: Hydrolase]]
[[Category: Ligase-dna complex]]
[[Category: Ligase/dna]]
[[Category: Protein-dna complex]]
[[Category: Recombination]]
[[Category: Site-specific recombinase]]
[[Category: Three-way junction]]
[[Category: Trimeric]]
[[Category: Y-junction]]

Latest revision as of 10:10, 7 February 2024

CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEXCRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX

Structural highlights

1f44 is a 3 chain structure with sequence from Escherichia virus P1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.05Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1f44, resolution 2.05Å

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