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| | <StructureSection load='5fox' size='340' side='right'caption='[[5fox]], [[Resolution|resolution]] 1.30Å' scene=''> | | <StructureSection load='5fox' size='340' side='right'caption='[[5fox]], [[Resolution|resolution]] 1.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fox]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FOX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FOX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fox]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FOX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fos|5fos]], [[5fot|5fot]], [[5fou|5fou]], [[5fov|5fov]], [[5fow|5fow]]</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=5fox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fox OCA], [https://pdbe.org/5fox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fox RCSB], [https://www.ebi.ac.uk/pdbsum/5fox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fox 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=5fox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fox OCA], [http://pdbe.org/5fox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fox RCSB], [http://www.ebi.ac.uk/pdbsum/5fox PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fox ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RADA_PYRFU RADA_PYRFU]] Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules. | + | [https://www.uniprot.org/uniprot/RADA_PYRFU RADA_PYRFU] Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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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: Atcc 43587]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Abell, C]] | + | [[Category: Pyrococcus furiosus]] |
| - | [[Category: Blundell, T L]] | + | [[Category: Abell C]] |
| - | [[Category: Hyvonen, M]] | + | [[Category: Blundell TL]] |
| - | [[Category: Marsh, M]] | + | [[Category: Hyvonen M]] |
| - | [[Category: Scott, D E]] | + | [[Category: Marsh M]] |
| - | [[Category: Fxxa motif]]
| + | [[Category: Scott DE]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Rada]]
| + | |
| - | [[Category: Recombinase]]
| + | |
| Structural highlights
Function
RADA_PYRFU Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules.
Publication Abstract from PubMed
RAD51 is a recombinase involved in the homologous recombination of double-strand breaks in DNA. RAD51 forms oligomers by binding to another molecule of RAD51 via an 'FxxA' motif, and the same recognition sequence is similarly utilised to bind BRCA2. We have tabulated the effects of mutation of this sequence, across a variety of experimental methods and from relevant mutations observed in the clinic. We use mutants of a tetrapeptide sequence to probe the binding interaction, using both isothermal titration calorimetry and X-ray crystallography. Where possible, comparison between our tetrapeptide mutational study and the previously reported mutations is made, discrepancies are discussed and the importance of secondary structure in interpreting alanine scanning and mutational data of this nature is considered.
Structure-activity relationship of the peptide binding-motif mediating the BRCA2:RAD51 protein-protein interaction.,Scott DE, Marsh M, Blundell TL, Abell C, Hyvonen M FEBS Lett. 2016 Apr;590(8):1094-102. doi: 10.1002/1873-3468.12139. Epub 2016 Apr , 6. PMID:26992456[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Scott DE, Marsh M, Blundell TL, Abell C, Hyvonen M. Structure-activity relationship of the peptide binding-motif mediating the BRCA2:RAD51 protein-protein interaction. FEBS Lett. 2016 Apr;590(8):1094-102. doi: 10.1002/1873-3468.12139. Epub 2016 Apr , 6. PMID:26992456 doi:http://dx.doi.org/10.1002/1873-3468.12139
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