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| | <StructureSection load='3lda' size='340' side='right'caption='[[3lda]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='3lda' size='340' side='right'caption='[[3lda]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3lda]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LDA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LDA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3lda]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LDA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LDA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1szp|1szp]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAD51, YER095W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3lda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lda OCA], [https://pdbe.org/3lda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lda RCSB], [https://www.ebi.ac.uk/pdbsum/3lda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lda 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=3lda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lda OCA], [https://pdbe.org/3lda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lda RCSB], [https://www.ebi.ac.uk/pdbsum/3lda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lda ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RAD51_YEAST RAD51_YEAST]] Required both for recombination and for the repair of DNA damage caused by X-rays. Its function may be modulated by interaction with other repair proteins. RAD52 interacts directly with RAD51, via its C-terminus. Forms a nucleoprotein filament with DNA as an early intermediate in recombination.<ref>PMID:16818607</ref>
| + | [https://www.uniprot.org/uniprot/RAD51_YEAST RAD51_YEAST] Required both for recombination and for the repair of DNA damage caused by X-rays. Its function may be modulated by interaction with other repair proteins. RAD52 interacts directly with RAD51, via its C-terminus. Forms a nucleoprotein filament with DNA as an early intermediate in recombination.<ref>PMID:16818607</ref> |
| | == 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: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, J]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Morrical, S W]] | + | [[Category: Chen J]] |
| - | [[Category: Rould, M A]] | + | [[Category: Morrical SW]] |
| - | [[Category: Villanueva, N L]] | + | [[Category: Rould MA]] |
| - | [[Category: Atp-binding]] | + | [[Category: Villanueva NL]] |
| - | [[Category: Atp-hydrolysis]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dna damage]]
| + | |
| - | [[Category: Dna recombination]]
| + | |
| - | [[Category: Dna repair]]
| + | |
| - | [[Category: Non-prolyl cis peptide]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Walker a/b]]
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| Structural highlights
Function
RAD51_YEAST Required both for recombination and for the repair of DNA damage caused by X-rays. Its function may be modulated by interaction with other repair proteins. RAD52 interacts directly with RAD51, via its C-terminus. Forms a nucleoprotein filament with DNA as an early intermediate in recombination.[1]
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
Rad51 protein promotes homologous recombination in eukaryotes. Recombination activities are activated by Rad51 filament assembly on ssDNA. Previous studies of yeast Rad51 showed that His352 occupies an important position at the filament interface, where it could relay signals between subunits and active sites. To investigate, we characterized yeast Rad51 H352A and H352Y mutants, and solved the structure of H352Y. H352A forms catalytically competent but salt-labile complexes on ssDNA. In contrast, H352Y forms salt-resistant complexes on ssDNA, but is defective in nucleotide exchange, RPA displacement and strand exchange with full-length DNA substrates. The 2.5 A crystal structure of H352Y reveals a right-handed helical filament in a high-pitch (130 A) conformation with P6(1) symmetry. The catalytic core and dimer interface regions of H352Y closely resemble those of DNA-bound Escherichia coli RecA protein. The H352Y mutation stabilizes Phe187 from the adjacent subunit in a position that interferes with the gamma-phosphate-binding site of the Walker A motif/P-loop, potentially explaining the limited catalysis observed. Comparison of Rad51 H352Y, RecA-DNA and related structures reveals that the presence of bound DNA correlates with the isomerization of a conserved cis peptide near Walker B to the trans configuration, which appears to prime the catalytic glutamate residue for ATP hydrolysis.
Insights into the mechanism of Rad51 recombinase from the structure and properties of a filament interface mutant.,Chen J, Villanueva N, Rould MA, Morrical SW Nucleic Acids Res. 2010 Aug;38(14):4889-906. Epub 2010 Apr 5. PMID:20371520[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tsubouchi H, Roeder GS. Budding yeast Hed1 down-regulates the mitotic recombination machinery when meiotic recombination is impaired. Genes Dev. 2006 Jul 1;20(13):1766-75. PMID:16818607 doi:20/13/1766
- ↑ Chen J, Villanueva N, Rould MA, Morrical SW. Insights into the mechanism of Rad51 recombinase from the structure and properties of a filament interface mutant. Nucleic Acids Res. 2010 Aug;38(14):4889-906. Epub 2010 Apr 5. PMID:20371520 doi:10.1093/nar/gkq209
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