2l90 | pdb_00002l90

Solution structure of murine myristoylated msrA

spinqualitylabelsall models 2l90, 21 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2l90 is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MYR Gene: Msra (Mus musculus) Activity: Peptide-methionine (S)-S-oxide reductase, with EC number 1.8.4.11 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase a.,Lim JC, Gruschus JM, Ghesquiere B, Kim G, Piszczek G, Tjandra N, Levine RL J Biol Chem. 2012 Jul 20;287(30):25589-95. Epub 2012 Jun 1. PMID:22661718 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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