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TitleCryogenic electron microscopy structures reveal how ATP and DNA binding in MutS coordinates sequential steps of DNA mismatch repair.
Journal, issue, pagesNat Struct Mol Biol, Vol. 29, Issue 1, Page 59-66, Year 2022
Publish dateJan 10, 2022
AuthorsAlessandro Borsellini / Vladislav Kunetsky / Peter Friedhoff / Meindert H Lamers /
PubMed AbstractDNA mismatch repair detects and corrects mismatches introduced during DNA replication. The protein MutS scans for mismatches and coordinates the repair cascade. During this process, MutS undergoes ...DNA mismatch repair detects and corrects mismatches introduced during DNA replication. The protein MutS scans for mismatches and coordinates the repair cascade. During this process, MutS undergoes multiple conformational changes in response to ATP binding, hydrolysis and release, but how ATP induces the various MutS conformations is incompletely understood. Here we present four cryogenic electron microscopy structures of Escherichia coli MutS at sequential stages of the ATP hydrolysis cycle that reveal how ATP binding and hydrolysis induce closing and opening of the MutS dimer, respectively. Biophysical analysis demonstrates how DNA binding modulates the ATPase cycle by prevention of hydrolysis during scanning and mismatch binding, while preventing ADP release in the sliding clamp state. Nucleotide release is achieved when MutS encounters single-stranded DNA that is produced during removal of the daughter strand. The combination of ATP binding and hydrolysis and its modulation by DNA enables MutS to adopt the different conformations needed to coordinate the sequential steps of the mismatch repair cascade.
External linksNat Struct Mol Biol / PubMed:35013597
MethodsEM (single particle)
Resolution3.3 - 4.8 Å
Structure data

13063

7oto

EMDB-13063, PDB-7oto:
The structure of MutS bound to two molecules of AMPPNP
Method: EM (single particle) / Resolution: 3.4 Å

13071

7ou0

EMDB-13071, PDB-7ou0:
The structure of MutS bound to two molecules of ADP-Vanadate
Method: EM (single particle) / Resolution: 3.8 Å

13073

7ou2

EMDB-13073, PDB-7ou2:
The structure of MutS bound to two molecules of ADP
Method: EM (single particle) / Resolution: 4.8 Å

13074

7ou4

EMDB-13074, PDB-7ou4:
The structure of MutS bound to one molecule of ATP and one molecule of ADP
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-VO4:
VANADATE ION / Vanadate

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

Source
  • escherichia coli (E. coli)
  • escherichia coli (strain k12) (bacteria)
KeywordsDNA BINDING PROTEIN / DNA mismatch repair protein

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