1ng9
From Proteopedia
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E.coli MutS R697A: an ATPase-asymmetry mutant
Overview
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.
About this Structure
1NG9 is a Single protein structure of sequence from Escherichia coli with MG and ADP as ligands. Full crystallographic information is available from OCA.
Reference
The alternating ATPase domains of MutS control DNA mismatch repair., Lamers MH, Winterwerp HH, Sixma TK, EMBO J. 2003 Feb 3;22(3):746-56. PMID:12554674
Page seeded by OCA on Tue Nov 20 22:13:51 2007
