7E5W

The structure of CcpA from Staphylococcus aureus

7E5W の概要

• エントリーDOI: 10.2210/pdb7e5w/pdb
• 分子名称: Catabolite control protein A, SULFATE ION (3 entities in total)
• 機能のキーワード: dimer, dna binding protein, regulater
• 由来する生物種: Staphylococcus aureus (strain N315)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 108885.88

構造登録者

Yu, G.,Wei, X. (登録日: 2021-02-20, 公開日: 2021-07-14, 最終更新日: 2023-11-29)

主引用文献

Liao, X.,Li, H.,Guo, Y.,Yang, F.,Chen, Y.,He, X.,Li, H.,Xia, W.,Mao, Z.W.,Sun, H.
Regulation of DNA-binding activity of the Staphylococcus aureus catabolite control protein A by copper (II)-mediated oxidation.
J.Biol.Chem., 298:101587-101587, 2022

PubMed Abstract: Catabolite control protein A (CcpA) of the human pathogen Staphylococcus aureus is an essential DNA regulator for carbon catabolite repression and virulence, which facilitates bacterial survival and adaptation to a changing environment. Here, we report that copper (II) signaling mediates the DNA-binding capability of CcpA in vitro and in vivo. Copper (II) catalyzes the oxidation of two cysteine residues (Cys216 and Cys242) in CcpA to form intermolecular disulfide bonds between two CcpA dimers, which results in the formation and dissociation of a CcpA tetramer of CcpA from its cognate DNA promoter. We further demonstrate that the two cysteine residues on CcpA are important for S. aureus to resist host innate immunity, indicating that S. aureus CcpA senses the redox-active copper (II) ions as a natural signal to cope with environmental stress. Together, these findings reveal a novel regulatory mechanism for CcpA activity through copper (II)-mediated oxidation.

PubMed: 35032550
DOI: 10.1016/j.jbc.2022.101587

実験手法

X-RAY DIFFRACTION (2.55 Å)