2bv6
From Proteopedia
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[[Category: virulence determinant]] | [[Category: virulence determinant]] | ||
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Revision as of 15:44, 5 November 2007
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CRYSTAL STRUCTURE OF MGRA, A GLOBAL REGULATOR AND MAJOR VIRULENCE DETERMINANT IN STAPHYLOCOCCUS AUREUS
Overview
Staphylococcus 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.
About this Structure
2BV6 is a Single protein structure of sequence from Staphylococcus aureus with SO4 as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
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
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