Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains
This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.
Feature 1:ATP binding site [chemical binding site]
Evidence:
Structure:4P7A: human MLH1 protomer binds ADP, contacts at 4A
Comment:human MLH1 can be roughly divided into two halves: an N-terminal HTPase domain, and a C-terminal domain which is the site of dimerization with MLH1 paralogs; in higher eukaryotes, the MLH1 and PMS2 paralogs form a heterodimeric complex
Comment:based on structures of the HATPase domain of human MLH1, human PMS2, human Hsp90, Escherichia coli DNA gyrase B, and other related proteins, bound with ATP, ADP or their analogs; contacts at 4A
Jiyao W et al.(2023). "The conserved domain database in 2023.",