1PPX
Solution Structure of the MutT Pyrophosphohydrolase Complexed with Mg(2+) and 8-oxo-dGMP, a Tightly-bound Product
Summary for 1PPX
| Entry DOI | 10.2210/pdb1ppx/pdb |
| Related | 1MUT 1TUM |
| NMR Information | BMRB: 5866 |
| Descriptor | Mutator mutT protein, MAGNESIUM ION, 8-OXO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | mutator protein, nucleoside triphosphate pyrophosphohydrolase, mutt pyrophosphohydrolase-metal-product complex, hydrolase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 15332.56 |
| Authors | Massiah, M.A.,Saraswat, V.,Azurmendi, H.F.,Mildvan, A.S. (deposition date: 2003-06-17, release date: 2003-08-26, Last modification date: 2024-05-22) |
| Primary citation | Massiah, M.A.,Saraswat, V.,Azurmendi, H.F.,Mildvan, A.S. Solution structure and NH exchange studies of the MutT pyrophosphohydrolase complexed with Mg(2+) and 8-oxo-dGMP, a tightly bound product. Biochemistry, 42:10140-10154, 2003 Cited by PubMed Abstract: To learn the structural basis for the unusually tight binding of 8-oxo-nucleotides to the MutT pyrophosphohydrolase of Escherichia coli (129 residues), the solution structure of the MutT-Mg(2+)-8-oxo-dGMP product complex (K(D) = 52 nM) was determined by standard 3-D heteronuclear NMR methods. Using 1746 NOEs (13.5 NOEs/residue) and 186 phi and psi values derived from backbone (15)N, Calpha, Halpha, and Cbeta chemical shifts, 20 converged structures were computed with NOE violations DOI: 10.1021/bi030105p PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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