2bv6
Crystal structure of MgrA, a global regulator and major virulence determinant in Staphylococcus aureusCrystal structure of MgrA, a global regulator and major virulence determinant in Staphylococcus aureus
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedStaphylococcus aureus is a human pathogen responsible for most wound and hospital-acquired infections. The protein MgrA is both an important virulence determinant during infection and a regulator of antibiotic resistance in S. aureus. The crystal structure of the MgrA homodimer, solved at 2.86 A, indicates the presence of a unique cysteine residue located at the interface of the protein dimer. We discovered that this cysteine residue can be oxidized by various reactive oxygen species, such as hydrogen peroxide and organic hydroperoxide. Cysteine oxidation leads to dissociation of MgrA from DNA and initiation of signaling pathways that turn on antibiotic resistance in S. aureus. The oxidation-sensing mechanism is typically used by bacteria to counter challenges of reactive oxygen and nitrogen species. Our study reveals that in S. aureus, MgrA adopts a similar mechanism but uses it to globally regulate different defensive pathways. An oxidation-sensing mechanism is used by the global regulator MgrA in Staphylococcus aureus.,Chen PR, Bae T, Williams WA, Duguid EM, Rice PA, Schneewind O, He C Nat Chem Biol. 2006 Nov;2(11):591-5. Epub 2006 Sep 17. PMID:16980961[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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