2l90
From Proteopedia
Solution structure of murine myristoylated msrA
Structural highlights
FunctionMSRA_MOUSE Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).[HAMAP-Rule:MF_01401] Publication Abstract from PubMedMethionine 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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