Structure of the periplasmic copper-binding protein CueP from Salmonella enterica serovar Typhimurium

Bo Young Yoon, Yong Hak Kim, Nahee Kim, Bo Young Yun, Jin Sik Kim, Joon Hee Lee, Hyun Soo Cho, Kangseok Lee, Nam Chul Ha

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Abstract

CueP was initially identified as a copper-resistance gene in Salmonella enterica serovar Typhimurium, which has evolved to survive in the phagosomes of macrophages. Recently, CueP was determined to be a periplasmic copper-binding protein and has been implicated in the transfer of copper ions to SodCII in the periplasm. In this study, the crystal structure of CueP has been determined, revealing a V-shaped dimeric structure. The conserved cysteine and histidine residues are clustered on the surface of one side of the C-terminal domain, suggesting that this cysteine- and histidine-rich region is related to the function of CueP. LC-MS/MS analysis established the presence of a disulfide bond between Cys96 and Cys176 under aerobic conditions. Subsequent biophysical analyses showed that the CueP protein binds copper and zinc, and the mutation of Cys104 to serine (C104S) dramatically reduced the binding affinity for copper and zinc, suggesting that the cysteine- and histidine-rich cluster is responsible for copper binding. This study provides a structural basis for the participation of CueP in the resistance of the intracellular pathogen Salmonella to copper.

Original languageEnglish
Pages (from-to)1867-1875
Number of pages9
JournalActa Crystallographica Section D: Biological Crystallography
Volume69
Issue number10
DOIs
Publication statusPublished - 2013 Oct 1

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Periplasmic Binding Proteins
Salmonella enterica
Copper
Histidine
Cysteine
Zinc
Periplasm
Phagosomes
Salmonella
Disulfides
Serine
Serogroup
copper-binding protein
Macrophages
Ions
Mutation
Genes

All Science Journal Classification (ASJC) codes

  • Structural Biology

Cite this

Yoon, Bo Young ; Kim, Yong Hak ; Kim, Nahee ; Yun, Bo Young ; Kim, Jin Sik ; Lee, Joon Hee ; Cho, Hyun Soo ; Lee, Kangseok ; Ha, Nam Chul. / Structure of the periplasmic copper-binding protein CueP from Salmonella enterica serovar Typhimurium. In: Acta Crystallographica Section D: Biological Crystallography. 2013 ; Vol. 69, No. 10. pp. 1867-1875.
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Structure of the periplasmic copper-binding protein CueP from Salmonella enterica serovar Typhimurium. / Yoon, Bo Young; Kim, Yong Hak; Kim, Nahee; Yun, Bo Young; Kim, Jin Sik; Lee, Joon Hee; Cho, Hyun Soo; Lee, Kangseok; Ha, Nam Chul.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 69, No. 10, 01.10.2013, p. 1867-1875.

Research output: Contribution to journalArticle

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AU - Yoon, Bo Young

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AU - Kim, Nahee

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AU - Kim, Jin Sik

AU - Lee, Joon Hee

AU - Cho, Hyun Soo

AU - Lee, Kangseok

AU - Ha, Nam Chul

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N2 - CueP was initially identified as a copper-resistance gene in Salmonella enterica serovar Typhimurium, which has evolved to survive in the phagosomes of macrophages. Recently, CueP was determined to be a periplasmic copper-binding protein and has been implicated in the transfer of copper ions to SodCII in the periplasm. In this study, the crystal structure of CueP has been determined, revealing a V-shaped dimeric structure. The conserved cysteine and histidine residues are clustered on the surface of one side of the C-terminal domain, suggesting that this cysteine- and histidine-rich region is related to the function of CueP. LC-MS/MS analysis established the presence of a disulfide bond between Cys96 and Cys176 under aerobic conditions. Subsequent biophysical analyses showed that the CueP protein binds copper and zinc, and the mutation of Cys104 to serine (C104S) dramatically reduced the binding affinity for copper and zinc, suggesting that the cysteine- and histidine-rich cluster is responsible for copper binding. This study provides a structural basis for the participation of CueP in the resistance of the intracellular pathogen Salmonella to copper.

AB - CueP was initially identified as a copper-resistance gene in Salmonella enterica serovar Typhimurium, which has evolved to survive in the phagosomes of macrophages. Recently, CueP was determined to be a periplasmic copper-binding protein and has been implicated in the transfer of copper ions to SodCII in the periplasm. In this study, the crystal structure of CueP has been determined, revealing a V-shaped dimeric structure. The conserved cysteine and histidine residues are clustered on the surface of one side of the C-terminal domain, suggesting that this cysteine- and histidine-rich region is related to the function of CueP. LC-MS/MS analysis established the presence of a disulfide bond between Cys96 and Cys176 under aerobic conditions. Subsequent biophysical analyses showed that the CueP protein binds copper and zinc, and the mutation of Cys104 to serine (C104S) dramatically reduced the binding affinity for copper and zinc, suggesting that the cysteine- and histidine-rich cluster is responsible for copper binding. This study provides a structural basis for the participation of CueP in the resistance of the intracellular pathogen Salmonella to copper.

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