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 language | English |
|---|---|
| Pages (from-to) | 1867-1875 |
| Number of pages | 9 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 69 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - 2013 Oct 1 |
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All Science Journal Classification (ASJC) codes
- Structural Biology
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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 journal › Article
TY - JOUR
T1 - Structure of the periplasmic copper-binding protein CueP from Salmonella enterica serovar Typhimurium
AU - Yoon, Bo Young
AU - Kim, Yong Hak
AU - Kim, Nahee
AU - Yun, Bo Young
AU - Kim, Jin Sik
AU - Lee, Joon Hee
AU - Cho, Hyun Soo
AU - Lee, Kangseok
AU - Ha, Nam Chul
PY - 2013/10/1
Y1 - 2013/10/1
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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U2 - 10.1107/S090744491301531X
DO - 10.1107/S090744491301531X
M3 - Article
VL - 69
SP - 1867
EP - 1875
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 0907-4449
IS - 10
ER -