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| | <StructureSection load='4a6p' size='340' side='right'caption='[[4a6p]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='4a6p' size='340' side='right'caption='[[4a6p]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4a6p]] is a 1 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=4A6P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A6P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4a6p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A6P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.498Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pzn|1pzn]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4a6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a6p OCA], [http://pdbe.org/4a6p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a6p RCSB], [http://www.ebi.ac.uk/pdbsum/4a6p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a6p 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=4a6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a6p OCA], [https://pdbe.org/4a6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a6p RCSB], [https://www.ebi.ac.uk/pdbsum/4a6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a6p 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: Large Structures]] |
| - | [[Category: Abell, C]] | + | [[Category: Pyrococcus furiosus]] |
| - | [[Category: Blundell, T L]] | + | [[Category: Abell C]] |
| - | [[Category: Ehebauer, M T]] | + | [[Category: Blundell TL]] |
| - | [[Category: Hyvonen, M]] | + | [[Category: Ehebauer MT]] |
| - | [[Category: Marsh, M E]] | + | [[Category: Hyvonen M]] |
| - | [[Category: Scott, D]] | + | [[Category: Marsh ME]] |
| - | [[Category: Hydrolase]]
| + | [[Category: Scott D]] |
| - | [[Category: Recombinase]]
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| 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
Homologous recombination is essential for repair of DNA double-strand breaks. Central to this process is a family of recombinases, including archeal RadA and human RAD51, which form nucleoprotein filaments on damaged single-stranded DNA ends and facilitate their ATP-dependent repair. ATP binding and hydrolysis are dependent on the formation of a nucleoprotein filament comprising RadA/RAD51 and single-stranded DNA, with ATP bound between adjacent protomers. We demonstrate that truncated, monomeric Pyrococcus furiosus RadA and monomerised human RAD51 retain the ability to bind ATP and other nucleotides with high affinity. We present crystal structures of both apo and nucleotide-bound forms of monomeric RadA. These structures reveal that while phosphate groups are tightly bound, RadA presents a shallow, poorly defined binding surface for the nitrogenous bases of nucleotides. We suggest that RadA monomers would be constitutively bound to nucleotides in the cell and that the bound nucleotide might play a structural role in filament assembly.
ATP half-sites in RadA and RAD51 recombinases bind nucleotides.,Marsh ME, Scott DE, Ehebauer MT, Abell C, Blundell TL, Hyvonen M FEBS Open Bio. 2016 Apr 6;6(5):372-85. doi: 10.1002/2211-5463.12052. eCollection , 2016 May. PMID:27419043[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Marsh ME, Scott DE, Ehebauer MT, Abell C, Blundell TL, Hyvonen M. ATP half-sites in RadA and RAD51 recombinases bind nucleotides. FEBS Open Bio. 2016 Apr 6;6(5):372-85. doi: 10.1002/2211-5463.12052. eCollection , 2016 May. PMID:27419043 doi:http://dx.doi.org/10.1002/2211-5463.12052
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