MutS-1
| MutS_I | |||||||||
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MutS is a mismatch DNA repair protein, originally described in Escherichia coli.
loops produced during DNA replication.[1]
MutS and MutL are involved in preventing
structure. Mismatch binding induces ATP uptake and a conformational change in the MutS protein, resulting in a clamp that translocates
on DNA.
MutS is a modular protein with a complex structure,[5] and is composed of:
- N-terminal mismatch-recognition domain, which is similar in structure to tRNA endonuclease.
- Connector domain, which is similar in structureto Holliday junction resolvase ruvC.
- Core domain, which is composed of two separate subdomains that join together to form a helical bundle; from within the core domain, two helices act as levers that extend towards (but do not touch) the DNA.
- Clamp domain, which is inserted between the two subdomains of the core structure.
- ATPase domain (connected to the core domain), which has a classical Walker A motif.
- HTH (helix-turn-helix) domain, which is involved in dimer contacts.
mitochondria and chloroplasts.[7]
This entry represents the N-terminal domain of proteins in the MutS family of DNA mismatch repair proteins, as well as closely related proteins. The N-terminal domain of MutS is responsible for mismatch recognition and forms a 6-stranded mixed beta-sheet surrounded by three alpha-helices, which is similar to the
Human MSH has been implicated in non-polyposis colorectal carcinoma
(HNPCC) and is a mismatch binding protein.