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| | ==Structure of recombination mediator protein RecRK21G mutant== | | ==Structure of recombination mediator protein RecRK21G mutant== |
| - | <StructureSection load='3vdu' size='340' side='right' caption='[[3vdu]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='3vdu' size='340' side='right'caption='[[3vdu]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vdu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis Caldanaerobacter subterraneus subsp. tengcongensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VDU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VDU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vdu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis_MB4 Caldanaerobacter subterraneus subsp. tengcongensis MB4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VDU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vdp|3vdp]], [[3vds|3vds]], [[3vdt|3vdt]], [[3ve5|3ve5]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">recR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273068 Caldanaerobacter subterraneus subsp. tengcongensis])</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=3vdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vdu OCA], [https://pdbe.org/3vdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vdu RCSB], [https://www.ebi.ac.uk/pdbsum/3vdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vdu 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=3vdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vdu OCA], [http://pdbe.org/3vdu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vdu RCSB], [http://www.ebi.ac.uk/pdbsum/3vdu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vdu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RECR_CALS4 RECR_CALS4]] May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.[HAMAP-Rule:MF_00017] | + | [https://www.uniprot.org/uniprot/RECR_CALS4 RECR_CALS4] May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.[HAMAP-Rule:MF_00017] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Caldanaerobacter subterraneus subsp. tengcongensis]] | + | [[Category: Caldanaerobacter subterraneus subsp. tengcongensis MB4]] |
| - | [[Category: Liang, D C]] | + | [[Category: Large Structures]] |
| - | [[Category: Tang, Q]] | + | [[Category: Liang DC]] |
| - | [[Category: Yan, X X]] | + | [[Category: Tang Q]] |
| - | [[Category: Dna binding]] | + | [[Category: Yan XX]] |
| - | [[Category: Dna repair]]
| + | |
| - | [[Category: Recombination]]
| + | |
| - | [[Category: Zinc finger]]
| + | |
| Structural highlights
Function
RECR_CALS4 May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.[HAMAP-Rule:MF_00017]
Publication Abstract from PubMed
RecR is an important recombination mediator protein in the RecFOR pathway. RecR together with RecO and RecF facilitates RecA nucleoprotein filament formation and homologous pairing. Structural and biochemical studies of Thermoanaerobacter tengcongensis RecR (TTERecR) and its series mutants revealed that TTERecR uses the N-N dimer as a basic functional unit to interact with TTERecO monomer. Two TTERecR N-N dimers form a ring-shaped tetramer via an interaction between their C-terminal regions. The tetramer is a result of crystallization only. Hydrophobic interactions between the entire helix-hairpin-helix domains within the N-terminal regions of two TTERecR monomers are necessary for formation of a RecR functional N-N dimer. The TTERecR N-N dimer conformation also affects formation of a hydrophobic patch, which creates a binding site for TTERecO in the TTERecR Toprim domain. In addition, we demonstrate that TTERecR does not bind single-stranded DNA (ssDNA) and binds double-stranded DNA very weakly, whereas TTERecOR complex can stably bind DNA, with a higher affinity for ssDNA than double-stranded DNA. Based on these results, we propose an interaction model for the RecOR:ssDNA complex.
RecOR complex including RecR N-N dimer and RecO monomer displays a high affinity for ssDNA.,Tang Q, Gao P, Liu YP, Gao A, An XM, Liu S, Yan XX, Liang DC Nucleic Acids Res. 2012 Nov 1;40(21):11115-25. doi: 10.1093/nar/gks889. Epub 2012, Sep 27. PMID:23019218[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tang Q, Gao P, Liu YP, Gao A, An XM, Liu S, Yan XX, Liang DC. RecOR complex including RecR N-N dimer and RecO monomer displays a high affinity for ssDNA. Nucleic Acids Res. 2012 Nov 1;40(21):11115-25. doi: 10.1093/nar/gks889. Epub 2012, Sep 27. PMID:23019218 doi:http://dx.doi.org/10.1093/nar/gks889
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