7vuk
From Proteopedia
Crystal Structure of the core region of Thermus thermophilus MutS2 complexed with ADP.
Structural highlights
FunctionMUTS2_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] Publication Abstract from PubMedMutS 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. 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[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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