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| | <StructureSection load='2zqe' size='340' side='right'caption='[[2zqe]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='2zqe' size='340' side='right'caption='[[2zqe]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zqe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZQE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zqe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZQE FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TTHA1645 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</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]] 1.7Å</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=2zqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zqe OCA], [https://pdbe.org/2zqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zqe RCSB], [https://www.ebi.ac.uk/pdbsum/2zqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zqe 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=2zqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zqe OCA], [https://pdbe.org/2zqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zqe RCSB], [https://www.ebi.ac.uk/pdbsum/2zqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zqe ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MUTS2_THET8 MUTS2_THET8]] Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity. Cleaves the phosphate backbone of oligodeoxynucleotides non-sequence-specifically at the 3' side of the phosphates. Preferably incises the branched DNA structures, especially the D-loop structure over the Holliday junction. Has ATPase activity. Binds to dsDNA but not to ssDNA.[HAMAP-Rule:MF_00092]<ref>PMID:15113836</ref> <ref>PMID:17215294</ref> <ref>PMID:17686785</ref> <ref>PMID:18838375</ref>
| + | [https://www.uniprot.org/uniprot/MUTS2_THET8 MUTS2_THET8] Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity. Cleaves the phosphate backbone of oligodeoxynucleotides non-sequence-specifically at the 3' side of the phosphates. Preferably incises the branched DNA structures, especially the D-loop structure over the Holliday junction. Has ATPase activity. Binds to dsDNA but not to ssDNA.[HAMAP-Rule:MF_00092]<ref>PMID:15113836</ref> <ref>PMID:17215294</ref> <ref>PMID:17686785</ref> <ref>PMID:18838375</ref> |
| | == 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: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thet8]] | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Fukui, K]] | + | [[Category: Fukui K]] |
| - | [[Category: Kitamura, Y]] | + | [[Category: Kitamura Y]] |
| - | [[Category: Kuramitsu, S]] | + | [[Category: Kuramitsu S]] |
| - | [[Category: Masui, R]] | + | [[Category: Masui R]] |
| - | [[Category: Nakagawa, N]] | + | [[Category: Nakagawa N]] |
| - | [[Category: Alpha/beta]]
| + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| Structural highlights
Function
MUTS2_THET8 Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity. Cleaves the phosphate backbone of oligodeoxynucleotides non-sequence-specifically at the 3' side of the phosphates. Preferably incises the branched DNA structures, especially the D-loop structure over the Holliday junction. Has ATPase activity. Binds to dsDNA but not to ssDNA.[HAMAP-Rule:MF_00092][1] [2] [3] [4]
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
DNA recombination events need to be strictly regulated, because an increase in the recombinational frequency causes unfavorable alteration of genetic information. Recent studies revealed the existence of a novel anti-recombination enzyme, MutS2. However, the mechanism by which MutS2 inhibits homologous recombination has been unknown. Previously, we found that Thermus thermophilus MutS2 (ttMutS2) harbors an endonuclease activity and that this activity is confined to the C-terminal domain, whose amino acid sequence is widely conserved in a variety of proteins with unknown function from almost all organisms ranging from bacteria to man. In this study, we determined the crystal structure of the ttMutS2 endonuclease domain at 1.7-angstroms resolution, which resembles the structure of the DNase I-like catalytic domain of Escherichia coli RNase E, a sequence-nonspecific endonuclease. The N-terminal domain of ttMutS2, however, recognized branched DNA structures, including the Holliday junction and D-loop structure, a primary intermediate in homologous recombination. The full-length of ttMutS2 digested the branched DNA structures at the junction. These results indicate that ttMutS2 suppresses homologous recombination through a novel mechanism involving resolution of early intermediates.
Crystal structure of MutS2 endonuclease domain and the mechanism of homologous recombination suppression.,Fukui K, Nakagawa N, Kitamura Y, Nishida Y, Masui R, Kuramitsu S J Biol Chem. 2008 Nov 28;283(48):33417-27. Epub 2008 Oct 6. PMID:18838375[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fukui K, Masui R, Kuramitsu S. Thermus thermophilus MutS2, a MutS paralogue, possesses an endonuclease activity promoted by MutL. J Biochem. 2004 Mar;135(3):375-84. PMID:15113836
- ↑ Fukui K, Kosaka H, Kuramitsu S, Masui R. Nuclease activity of the MutS homologue MutS2 from Thermus thermophilus is confined to the Smr domain. Nucleic Acids Res. 2007;35(3):850-60. Epub 2007 Jan 10. PMID:17215294 doi:http://dx.doi.org/10.1093/nar/gkl735
- ↑ Fukui K, Takahata Y, Nakagawa N, Kuramitsu S, Masui R. Analysis of a nuclease activity of catalytic domain of Thermus thermophilus MutS2 by high-accuracy mass spectrometry. Nucleic Acids Res. 2007;35(15):e100. Epub 2007 Aug 7. PMID:17686785 doi:http://dx.doi.org/10.1093/nar/gkm575
- ↑ Fukui K, Nakagawa N, Kitamura Y, Nishida Y, Masui R, Kuramitsu S. Crystal structure of MutS2 endonuclease domain and the mechanism of homologous recombination suppression. J Biol Chem. 2008 Nov 28;283(48):33417-27. Epub 2008 Oct 6. PMID:18838375 doi:10.1074/jbc.M806755200
- ↑ Fukui K, Nakagawa N, Kitamura Y, Nishida Y, Masui R, Kuramitsu S. Crystal structure of MutS2 endonuclease domain and the mechanism of homologous recombination suppression. J Biol Chem. 2008 Nov 28;283(48):33417-27. Epub 2008 Oct 6. PMID:18838375 doi:10.1074/jbc.M806755200
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