5crx: Difference between revisions
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<StructureSection load='5crx' size='340' side='right'caption='[[5crx]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='5crx' size='340' side='right'caption='[[5crx]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5crx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[5crx]] is a 4 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=5CRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CRX FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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=5crx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5crx OCA], [https://pdbe.org/5crx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5crx RCSB], [https://www.ebi.ac.uk/pdbsum/5crx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5crx 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=5crx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5crx OCA], [https://pdbe.org/5crx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5crx RCSB], [https://www.ebi.ac.uk/pdbsum/5crx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5crx 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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia virus P1]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gopaul DN]] | |||
[[Category: Gopaul | [[Category: Guo F]] | ||
[[Category: Guo | [[Category: Van Duyne GD]] | ||
[[Category: | |||
Latest revision as of 21:05, 20 September 2023
ASYMMETRIC DNA-BENDING IN THE CRE-LOXP SITE-SPECIFIC RECOMBINATION SYNAPSEASYMMETRIC DNA-BENDING IN THE CRE-LOXP SITE-SPECIFIC RECOMBINATION SYNAPSE
Structural highlights
FunctionRECR_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. Publication Abstract from PubMedCre recombinase catalyzes site-specific recombination between two 34-bp loxP sites in a variety of DNA substrates. At the start of the recombination pathway, the loxP sites are each bound by two recombinase molecules, and synapsis of the sites is mediated by Cre-Cre interactions. We describe the structures of synaptic complexes formed between a symmetrized loxP site and two Cre mutants that are defective in strand cleavage. The DNA in these complexes is bent sharply at a single base pair step at one end of the crossover region in a manner that is atypical of protein-induced DNA bends. A large negative roll (-49 degrees) and a positive tilt (16 degrees) open the major groove toward the center of the synapse and compress the minor groove toward the protein-DNA interface. The bend direction of the site appears to determine which of the two DNA substrate strands will be cleaved and exchanged in the initial stages of the recombination pathway. These results provide a structural basis for the observation that exchange of DNA strands proceeds in a defined order in some tyrosine recombinase systems. The Cre-loxS synaptic complex structure supports a model in which synapsis of the loxP sites results in formation of a Holliday junction-like DNA architecture that is maintained through the initial cleavage and strand exchange steps in the site-specific recombination pathway. Asymmetric DNA bending in the Cre-loxP site-specific recombination synapse.,Guo F, Gopaul DN, Van Duyne GD Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7143-8. PMID:10377382[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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