2BV6
Crystal structure of MgrA, a global regulator and major virulence determinant in Staphylococcus aureus
2BV6 の概要
| エントリーDOI | 10.2210/pdb2bv6/pdb |
| 分子名称 | HTH-TYPE TRANSCRIPTIONAL REGULATOR MGRA, SULFATE ION (3 entities in total) |
| 機能のキーワード | transcriptional regulator, multidrug resistance regulator, virulence determinant, transcriptional factors |
| 由来する生物種 | STAPHYLOCOCCUS AUREUS |
| 細胞内の位置 | Cytoplasm (Probable): Q7X448 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 16629.57 |
| 構造登録者 | Chen, P.R.,Bae, T.,Williams, W.A.,Duguid, E.M.,Rice, P.A.,Schneewind, O.,He, C. (登録日: 2005-06-22, 公開日: 2006-09-20, 最終更新日: 2024-11-13) |
| 主引用文献 | Chen, P.R.,Bae, T.,Williams, W.A.,Duguid, E.M.,Rice, P.A.,Schneewind, O.,He, C. An Oxidation-Sensing Mechanism is Used by the Global Regulator Mgra in Staphylococcus Aureus. Nat.Chem.Biol., 2:591-, 2006 Cited by PubMed Abstract: 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. PubMed: 16980961DOI: 10.1038/NCHEMBIO820 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






