7AIB
MutS-MutL in clamp state
Summary for 7AIB
| Entry DOI | 10.2210/pdb7aib/pdb |
| EMDB information | 11794 |
| Descriptor | DNA mismatch repair protein MutS, DNA mismatch repair protein MutL, DNA (30-MER), ... (5 entities in total) |
| Functional Keywords | dna mismatch repair muts, dna binding protein |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 5 |
| Total formula weight | 249248.06 |
| Authors | Fernandez-Leiro, R.,Bhairosing-Kok, D.,Sixma, T.K.,Lamers, M.H. (deposition date: 2020-09-26, release date: 2021-03-31, Last modification date: 2024-05-01) |
| Primary citation | Fernandez-Leiro, R.,Bhairosing-Kok, D.,Kunetsky, V.,Laffeber, C.,Winterwerp, H.H.,Groothuizen, F.,Fish, A.,Lebbink, J.H.G.,Friedhoff, P.,Sixma, T.K.,Lamers, M.H. The selection process of licensing a DNA mismatch for repair. Nat.Struct.Mol.Biol., 28:373-381, 2021 Cited by PubMed Abstract: DNA mismatch repair detects and removes mismatches from DNA by a conserved mechanism, reducing the error rate of DNA replication by 100- to 1,000-fold. In this process, MutS homologs scan DNA, recognize mismatches and initiate repair. How the MutS homologs selectively license repair of a mismatch among millions of matched base pairs is not understood. Here we present four cryo-EM structures of Escherichia coli MutS that provide snapshots, from scanning homoduplex DNA to mismatch binding and MutL activation via an intermediate state. During scanning, the homoduplex DNA forms a steric block that prevents MutS from transitioning into the MutL-bound clamp state, which can only be overcome through kinking of the DNA at a mismatch. Structural asymmetry in all four structures indicates a division of labor between the two MutS monomers. Together, these structures reveal how a small conformational change from the homoduplex- to heteroduplex-bound MutS acts as a licensing step that triggers a dramatic conformational change that enables MutL binding and initiation of the repair cascade. PubMed: 33820992DOI: 10.1038/s41594-021-00577-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.7 Å) |
Structure validation
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