7VUF
Crystal Structure of the core region of Thermus thermophilus MutS2.
Summary for 7VUF
| Entry DOI | 10.2210/pdb7vuf/pdb |
| Descriptor | Endonuclease MutS2, DI(HYDROXYETHYL)ETHER, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | atpase, hydrolase, dna binding protein |
| Biological source | Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) |
| Total number of polymer chains | 4 |
| Total formula weight | 217488.57 |
| Authors | |
| Primary citation | Fukui, K.,Inoue, M.,Murakawa, T.,Baba, S.,Kumasaka, T.,Yano, T. Structural and functional insights into the mechanism by which MutS2 recognizes a DNA junction. Structure, 30:973-982.e4, 2022 Cited by PubMed Abstract: 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. PubMed: 35439431DOI: 10.1016/j.str.2022.03.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.11 Å) |
Structure validation
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