1NG9

E.coli MutS R697A: an ATPase-asymmetry mutant

Summary for 1NG9

• Entry DOI: 10.2210/pdb1ng9/pdb
• Related: 1e3m 1ewq 1ewr 1fw6
• Descriptor: 5'-D(*AP*GP*CP*TP*GP*CP*CP*AP*GP*GP*CP*AP*CP*CP*AP*GP*TP*GP*TP*CP*AP*GP*CP*GP*TP*CP*CP*TP*AP*T)-3', 5'-D(*AP*TP*AP*GP*GP*AP*CP*GP*CP*TP*GP*AP*CP*AP*CP*TP*GP*GP*TP*GP*CP*TP*TP*GP*GP*CP*AP*GP*CP*T)-3', DNA mismatch repair protein MutS, ... (6 entities in total)
• Functional Keywords: abc atpase, alternating atpase, asymmetry, dna repair, dna binding, dna binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 198404.36

Authors

Lamers, M.H.,Winterwerp, H.H.K.,Sixma, T.K. (deposition date: 2002-12-17, release date: 2003-02-11, Last modification date: 2023-08-16)

Primary citation

Lamers, M.H.,Winterwerp, H.H.K.,Sixma, T.K.
The alternating ATPase domains of MutS control DNA mismatch repair
Embo J., 22:746-756, 2003

PubMed Abstract: DNA mismatch repair is an essential safeguard of genomic integrity by removing base mispairings that may arise from DNA polymerase errors or from homologous recombination between DNA strands. In Escherichia coli, the MutS enzyme recognizes mismatches and initiates repair. MutS has an intrinsic ATPase activity crucial for its function, but which is poorly understood. We show here that within the MutS homodimer, the two chemically identical ATPase sites have different affinities for ADP, and the two sites alternate in ATP hydrolysis. A single residue, Arg697, located at the interface of the two ATPase domains, controls the asymmetry. When mutated, the asymmetry is lost and mismatch repair in vivo is impaired. We propose that asymmetry of the ATPase domains is an essential feature of mismatch repair that controls the timing of the different steps in the repair cascade.

PubMed: 12554674
DOI: 10.1093/emboj/cdg064

Experimental method

X-RAY DIFFRACTION (2.6 Å)