Structure of Mycobacterium tuberculosis Methionine Sulfoxide Reductase A in Complex with Protein-Bound Methionine

Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine.

Peptide methionine sulfoxide reductase (MsrA) repairs oxidative damage to methionine residues arising from reactive oxygen species and reactive nitrogen intermediates. MsrA activity is found in a wide variety of organisms, and it is implicated as one of the primary defenses against oxidative stress. Disruption of the gene encoding MsrA in several pathogenic bacteria responsible for infections i...

Complex with Protein-Bound Methionine Methionine Sulfoxide Reductase A in Mycobacterium tuberculosis

Methionine sulfoxide reductase A is a stereospecific methionine oxidase.

Methionine sulfoxide reductase A (MsrA) catalyzes the reduction of methionine sulfoxide to methionine and is specific for the S epimer of methionine sulfoxide. The enzyme participates in defense against oxidative stresses by reducing methionine sulfoxide residues in proteins back to methionine. Because oxidation of methionine residues is reversible, this covalent modification could also functio...

A natural carbohydrate substrate for Mycobacterium tuberculosis methionine sulfoxide reductase A.

Enzymatic reduction of the methylsulfinylxylofuranosyl (MSX) groups in lipoarabinomannan provides proof of the absolute configuration of MSX and a possible biochemical mechanism for oxidative protection in Mycobacterium tuberculosis.

Selenium and the methionine sulfoxide reductase system.

Selenium is a chemical element participating in the synthesis of selenocysteine residues that play a pivotal role in the enzymatic activity efficiency of selenoproteines. The methionine sulfoxide reductase (Msr) system that reduces methionine sulfoxide (MetO) to methionine comprises the selenoprotein MsrB (MsrB1) and the non-selenoprotein MsrA, which reduce the R- and the S- forms of MetO, resp...