1w7a
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ATP BOUND MUTS
OverviewOverview
MutS is the key protein of the Escherichia coli DNA mismatch repair, system. It recognizes mispaired and unpaired bases and has intrinsic, ATPase activity. ATP binding after mismatch recognition by MutS serves as, a switch that enables MutL binding and the subsequent initiation of, mismatch repair. However, the mechanism of this switch is poorly, understood. We have investigated the effects of ATP binding on the MutS, structure. Crystallographic studies of ATP-soaked crystals of MutS show a, trapped intermediate, with ATP in the nucleotide-binding site. Local, rearrangements of several residues around the nucleotide-binding site, suggest a movement of the two ATPase domains of the MutS dimer toward each, other. Analytical ultracentrifugation experiments confirm such a, rearrangement, ... [(full description)]
About this StructureAbout this Structure
1W7A is a [Protein complex] structure of sequences from [Escherichia coli] with MG and ATP as [ligands]. Full crystallographic information is available from [OCA].
ReferenceReference
ATP increases the affinity between MutS ATPase domains. Implications for ATP hydrolysis and conformational changes., Lamers MH, Georgijevic D, Lebbink JH, Winterwerp HH, Agianian B, de Wind N, Sixma TK, J Biol Chem. 2004 Oct 15;279(42):43879-85. Epub 2004 Aug 4. PMID:15297450
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