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| <StructureSection load='7vuf' size='340' side='right'caption='[[7vuf]], [[Resolution|resolution]] 3.11Å' scene=''> | | <StructureSection load='7vuf' size='340' side='right'caption='[[7vuf]], [[Resolution|resolution]] 3.11Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[7vuf]] is a 4 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=7VUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VUF FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VUF FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 3.11Å</td></tr> |
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=7vuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vuf OCA], [https://pdbe.org/7vuf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vuf RCSB], [https://www.ebi.ac.uk/pdbsum/7vuf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vuf 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=7vuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vuf OCA], [https://pdbe.org/7vuf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vuf RCSB], [https://www.ebi.ac.uk/pdbsum/7vuf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vuf ProSAT]</span></td></tr> |
| </table> | | </table> |
| == 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>
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| MutS family proteins are classified into MutS-I and -II lineages: MutS-I recognizes mismatched DNA and initiates mismatch repair, whereas MutS-II recognizes DNA junctions to modulate recombination. MutS-I forms dimeric clamp-like structures enclosing the mismatched DNA, and its composite ATPase sites regulate DNA-binding modes. Meanwhile, the structures of MutS-II have not been determined; accordingly, it remains unknown how MutS-II recognizes DNA junctions and how nucleotides control DNA binding. Here, we solved the ligand-free and ADP-bound crystal structures of bacterial MutS2 belonging to MutS-II. MutS2 also formed a dimeric clamp-like structure with composite ATPase sites. The ADP-bound MutS2 was more flexible compared to the ligand-free form and could be more suitable for DNA entry. The inner hole of the MutS2 clamp was two times larger than that of MutS-I, and site-directed mutagenesis analyses revealed DNA-binding sites at the inner hole. Based on these, a model is proposed that describes how MutS2 recognizes DNA junctions.
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| Structural and functional insights into the mechanism by which MutS2 recognizes a DNA junction.,Fukui K, Inoue M, Murakawa T, Baba S, Kumasaka T, Yano T Structure. 2022 Jul 7;30(7):973-982.e4. doi: 10.1016/j.str.2022.03.014. Epub 2022, Apr 18. PMID:35439431<ref>PMID:35439431</ref>
| | ==See Also== |
| | | *[[Endonuclease 3D structures|Endonuclease 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 7vuf" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Thermus thermophilus HB8]]
| |
| [[Category: Fukui K]] | | [[Category: Fukui K]] |
| [[Category: Yano T]] | | [[Category: Yano T]] |