7vuk
From Proteopedia
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==Crystal Structure of the core region of Thermus thermophilus MutS2 complexed with ADP.== | ==Crystal Structure of the core region of Thermus thermophilus MutS2 complexed with ADP.== | ||
| - | <StructureSection load='7vuk' size='340' side='right'caption='[[7vuk]]' scene=''> | + | <StructureSection load='7vuk' size='340' side='right'caption='[[7vuk]], [[Resolution|resolution]] 3.38Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VUK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7vuk]] is a 2 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=7VUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VUK FirstGlance]. <br> |
| - | </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=7vuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vuk OCA], [https://pdbe.org/7vuk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vuk RCSB], [https://www.ebi.ac.uk/pdbsum/7vuk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vuk ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=7vuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vuk OCA], [https://pdbe.org/7vuk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vuk RCSB], [https://www.ebi.ac.uk/pdbsum/7vuk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vuk 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7vuk" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__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]] | ||
Revision as of 19:34, 19 October 2022
Crystal Structure of the core region of Thermus thermophilus MutS2 complexed with ADP.
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