2WTU
Crystal structure of Escherichia coli MutS in complex with a 16 basepair oligo containing an A.A mismatch.
Summary for 2WTU
| Entry DOI | 10.2210/pdb2wtu/pdb |
| Related | 1E3M 1NG9 1OH5 1OH6 1OH7 1OH8 1W7A 1WB9 1WBB 1WBD |
| Descriptor | DNA MISMATCH REPAIR PROTEIN MUTS, DNA, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total) |
| Functional Keywords | dna binding protein-dna complex, dna damage, dna repair, nucleotide-binding, dna binding protein/dna |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 189549.65 |
| Authors | Natrajan, G.,Lebbink, J.H.,Reumer, A.,Fish, A.,Winterwerp, H.H.,Sixma, T.K. (deposition date: 2009-09-22, release date: 2010-02-09, Last modification date: 2023-12-20) |
| Primary citation | Lebbink, J.H.,Fish, A.,Reumer, A.,Natrajan, G.,Winterwerp, H.H.,Sixma, T.K. Magnesium coordination controls the molecular switch function of DNA mismatch repair protein MutS. J. Biol. Chem., 285:13131-13141, 2010 Cited by PubMed Abstract: The DNA mismatch repair protein MutS acts as a molecular switch. It toggles between ADP and ATP states and is regulated by mismatched DNA. This is analogous to G-protein switches and the regulation of their "on" and "off" states by guanine exchange factors. Although GDP release in monomeric GTPases is accelerated by guanine exchange factor-induced removal of magnesium from the catalytic site, we found that release of ADP from MutS is not influenced by the metal ion in this manner. Rather, ADP release is induced by the binding of mismatched DNA at the opposite end of the protein, a long-range allosteric response resembling the mechanism of activation of heterotrimeric GTPases. Magnesium influences switching in MutS by inducing faster and tighter ATP binding, allowing rapid downstream responses. MutS mutants with decreased affinity for the metal ion are impaired in fast switching and in vivo mismatch repair. Thus, the G-proteins and MutS conceptually employ the same efficient use of the high energy cofactor: slow hydrolysis in the absence of a signal and fast conversion to the active state when required. PubMed: 20167596DOI: 10.1074/jbc.M109.066001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
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