7E5W

The structure of CcpA from Staphylococcus aureus

Summary for 7E5W

• Entry DOI: 10.2210/pdb7e5w/pdb
• Descriptor: Catabolite control protein A, SULFATE ION (3 entities in total)
• Functional Keywords: dimer, dna binding protein, regulater
• Biological source: Staphylococcus aureus (strain N315)
• Total number of polymer chains: 3
• Total formula weight: 108885.88

Authors

Yu, G.,Wei, X. (deposition date: 2021-02-20, release date: 2021-07-14, Last modification date: 2023-11-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.55 Å)