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| | ==X-ray crystal structure of RecX== | | ==X-ray crystal structure of RecX== |
| - | <StructureSection load='3c1d' size='340' side='right' caption='[[3c1d]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='3c1d' size='340' side='right'caption='[[3c1d]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3c1d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C1D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C1D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3c1d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C1D FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">recX, oraA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">recX, oraA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=3c1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c1d OCA], [http://pdbe.org/3c1d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c1d RCSB], [http://www.ebi.ac.uk/pdbsum/3c1d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c1d 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=3c1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c1d OCA], [https://pdbe.org/3c1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c1d RCSB], [https://www.ebi.ac.uk/pdbsum/3c1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c1d ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RECX_ECO57 RECX_ECO57]] Modulates RecA activity through direct physical interaction. Can inhibit both RecA recombinase and coprotease activities. May have a regulatory role during the SOS response. Inhibits DNA strand exchange in vitro (By similarity). | + | [[https://www.uniprot.org/uniprot/RECX_ECO57 RECX_ECO57]] Modulates RecA activity through direct physical interaction. Can inhibit both RecA recombinase and coprotease activities. May have a regulatory role during the SOS response. Inhibits DNA strand exchange in vitro (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Furnham, N]] | | [[Category: Furnham, N]] |
| | [[Category: Maman, J D]] | | [[Category: Maman, J D]] |
| Structural highlights
Function
[RECX_ECO57] Modulates RecA activity through direct physical interaction. Can inhibit both RecA recombinase and coprotease activities. May have a regulatory role during the SOS response. Inhibits DNA strand exchange in vitro (By similarity).
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
The RecA/RAD51 nucleoprotein filament is central to the reaction of homologous recombination (HR). Filament activity must be tightly regulated in vivo as unrestrained HR can cause genomic instability. Our mechanistic understanding of HR is restricted by lack of structural information about the regulatory proteins that control filament activity. Here, we describe a structural and functional analysis of the HR inhibitor protein RecX and its mode of interaction with the RecA filament. RecX is a modular protein assembled of repeated three-helix motifs. The relative arrangement of the repeats generates an elongated and curved shape that is well suited for binding within the helical groove of the RecA filament. Structure-based mutagenesis confirms that conserved basic residues on the concave side of RecX are important for repression of RecA activity. Analysis of RecA filament dynamics in the presence of RecX shows that RecX actively promotes filament disassembly. Collectively, our data support a model in which RecX binding to the helical groove of the filament causes local dissociation of RecA protomers, leading to filament destabilisation and HR inhibition.
Structural basis for inhibition of homologous recombination by the RecX protein.,Ragone S, Maman JD, Furnham N, Pellegrini L EMBO J. 2008 Aug 20;27(16):2259-69. Epub 2008 Jul 24. PMID:18650935[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ragone S, Maman JD, Furnham N, Pellegrini L. Structural basis for inhibition of homologous recombination by the RecX protein. EMBO J. 2008 Aug 20;27(16):2259-69. Epub 2008 Jul 24. PMID:18650935 doi:10.1038/emboj.2008.145
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