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| | ==Cre recombinase-DNA transition state== | | ==Cre recombinase-DNA transition state== |
| - | <StructureSection load='3mgv' size='340' side='right' caption='[[3mgv]], [[Resolution|resolution]] 2.29Å' scene=''> | + | <StructureSection load='3mgv' size='340' side='right'caption='[[3mgv]], [[Resolution|resolution]] 2.29Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3mgv]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpp1 Bpp1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MGV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MGV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3mgv]] is a 12 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=3MGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MGV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></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]] 2.29Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1crx|1crx]], [[2hof|2hof]], [[2hoi|2hoi]], [[4crx|4crx]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cre ([http://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=3mgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mgv OCA], [https://pdbe.org/3mgv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mgv RCSB], [https://www.ebi.ac.uk/pdbsum/3mgv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mgv ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mgv OCA], [http://pdbe.org/3mgv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mgv RCSB], [http://www.ebi.ac.uk/pdbsum/3mgv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mgv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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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| | ==See Also== | | ==See Also== |
| - | *[[Resolvase|Resolvase]] | + | *[[Resolvase 3D structures|Resolvase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpp1]] | + | [[Category: Escherichia virus P1]] |
| - | [[Category: Chen, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Duyne, G D.Van]] | + | [[Category: Chen J]] |
| - | [[Category: Ghosh, K]] | + | [[Category: Ghosh K]] |
| - | [[Category: Gibb, B P]] | + | [[Category: Gibb BP]] |
| - | [[Category: Gupta, K]] | + | [[Category: Gupta K]] |
| - | [[Category: Sharp, R]] | + | [[Category: Sharp R]] |
| - | [[Category: Cre-loxp]] | + | [[Category: Van Duyne GD]] |
| - | [[Category: Isomerase-dna complex]]
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| - | [[Category: Transition state]]
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| Structural highlights
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.
Publication Abstract from PubMed
Members of the tyrosine recombinase (YR) family of site-specific recombinases catalyze DNA rearrangements using phosphoryl transfer chemistry that is identical to that used by the type IB topoisomerases (TopIBs). To better understand the requirements for YR catalysis and the relationship between the YRs and the TopIBs, we have analyzed the in vivo and in vitro recombination activities of all substitutions of the seven active site residues in Cre recombinase. We have also determined the structure of a vanadate transition state mimic for the Cre-loxP reaction that facilitates interpretation of mutant activities and allows for a comparison with similar structures from the related topoisomerases. We find that active site residues shared by the TopIBs are most sensitive to substitution. Only two, the tyrosine nucleophile and a conserved lysine residue that activates the 5'-hydroxyl leaving group, are strictly required to achieve >5% of wild-type activity. The two conserved arginine residues each tolerate one substitution that results in modest recombination activity and the remaining three active site positions can be substituted with several alternative amino acids while retaining a significant amount of activity. The results are discussed in the context of YR and TopIB structural models and data from related YR systems.
Requirements for catalysis in the Cre recombinase active site.,Gibb B, Gupta K, Ghosh K, Sharp R, Chen J, Van Duyne GD Nucleic Acids Res. 2010 May 12. PMID:20462863[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gibb B, Gupta K, Ghosh K, Sharp R, Chen J, Van Duyne GD. Requirements for catalysis in the Cre recombinase active site. Nucleic Acids Res. 2010 May 12. PMID:20462863 doi:10.1093/nar/gkq384
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