2L90
Solution structure of murine myristoylated msrA
Summary for 2L90
| Entry DOI | 10.2210/pdb2l90/pdb |
| NMR Information | BMRB: 17432 |
| Descriptor | Peptide methionine sulfoxide reductase, MYRISTIC ACID (2 entities in total) |
| Functional Keywords | oxidoreductase |
| Biological source | Mus musculus (mouse) |
| Cellular location | Isoform 1: Mitochondrion. Isoform 2: Cytoplasm: Q9D6Y7 |
| Total number of polymer chains | 1 |
| Total formula weight | 23907.94 |
| Authors | Gruschus, J.M.,Lim, J.,Piszczek, G.,Levine, R.L.,Tjandra, N. (deposition date: 2011-01-27, release date: 2012-01-11, Last modification date: 2024-11-06) |
| Primary citation | Lim, J.C.,Gruschus, J.M.,Ghesquiere, B.,Kim, G.,Piszczek, G.,Tjandra, N.,Levine, R.L. Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase A. J.Biol.Chem., 287:25589-25595, 2012 Cited by PubMed Abstract: Methionine sulfoxide reductase A is an essential enzyme in the antioxidant system which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide. The cytosolic form of the enzyme is myristoylated, but it is not known to translocate to membranes, and the function of myristoylation is not established. We compared the biochemical and biophysical properties of myristoylated and nonmyristoylated mouse methionine sulfoxide reductase A. These were almost identical for both forms of the enzyme, except that the myristoylated form reduced methionine sulfoxide in protein much faster than the nonmyristoylated form. We determined the solution structure of the myristoylated protein and found that the myristoyl group lies in a relatively surface exposed "myristoyl nest." We propose that this structure functions to enhance protein-protein interaction. PubMed: 22661718DOI: 10.1074/jbc.M112.368936 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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