Crystal structure of the copper chaperone for superoxide dismutase

A. L. Lamb; A. K. Wernimont; R. A. Pufahl; V. C. Culotta; T. V. O'Halloran; A. C. Rosenzweig

doi:10.1038/11489

Crystal structure of the copper chaperone for superoxide dismutase

A. L. Lamb, A. K. Wernimont, R. A. Pufahl, V. C. Culotta, T. V. O'Halloran, A. C. Rosenzweig^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

176 Scopus citations

Abstract

Cellular systems for handling transition metal ions have been identified, but little is known about the structure and function of the specific trafficking proteins. The 1.8 Å resolution structure of the yeast copper chaperone for superoxide dismutase (yCCS) reveals a protein composed of two domains. The N-terminal domain is very similar to the metallochaperone protein Atx1 and is likely to play a role in copper delivery and/or uptake. The second domain resembles the physiological target of yCCS, superoxide dismutase I (SOD1), in overall fold, but lacks all of the structural elements involved in catalysis. In the crystal, two SOD1-like domains interact to form a dimer. The subunit interface is remarkably similar to that in SOD1, suggesting a structural basis for target recognition by this metallochaperone.

Original language	English (US)
Pages (from-to)	724-729
Number of pages	6
Journal	Nature Structural Biology
Volume	6
Issue number	8
DOIs	https://doi.org/10.1038/11489
State	Published - 1999

ASJC Scopus subject areas

Structural Biology
Biochemistry
Genetics

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title = "Crystal structure of the copper chaperone for superoxide dismutase",

abstract = "Cellular systems for handling transition metal ions have been identified, but little is known about the structure and function of the specific trafficking proteins. The 1.8 {\AA} resolution structure of the yeast copper chaperone for superoxide dismutase (yCCS) reveals a protein composed of two domains. The N-terminal domain is very similar to the metallochaperone protein Atx1 and is likely to play a role in copper delivery and/or uptake. The second domain resembles the physiological target of yCCS, superoxide dismutase I (SOD1), in overall fold, but lacks all of the structural elements involved in catalysis. In the crystal, two SOD1-like domains interact to form a dimer. The subunit interface is remarkably similar to that in SOD1, suggesting a structural basis for target recognition by this metallochaperone.",

author = "Lamb, {A. L.} and Wernimont, {A. K.} and Pufahl, {R. A.} and Culotta, {V. C.} and O'Halloran, {T. V.} and Rosenzweig, {A. C.}",

note = "Funding Information: We thank L. Pascoli and M. Hou for assistance with crystallization and J. Quintana and D. Keane for assistance with data collection. This work was supported by a grant from the NIH (to A.C.R.), by funds from the ALS Association (A.C.R.), by funds from the Robert H. Lurie Cancer Center (A.C.R.), by a grant from the NIH (to T.V.O.), by a supplement from NIGMS to this same grant (to A.C.R. and T.V.O.), by funds from the ALS Association (T.V.O.), and by an NIH NRSA Training Grant (R.A.P.). The DND-CAT Synchrotron Research Center at the Advanced Photon Sourceis supported by the E.I. Dupont de Nemours & Co., The Dow Chemical Company, the NSF and the State of Illinois.",

year = "1999",

doi = "10.1038/11489",

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AU - Lamb, A. L.

AU - Wernimont, A. K.

AU - Pufahl, R. A.

AU - Culotta, V. C.

AU - O'Halloran, T. V.

AU - Rosenzweig, A. C.

N1 - Funding Information: We thank L. Pascoli and M. Hou for assistance with crystallization and J. Quintana and D. Keane for assistance with data collection. This work was supported by a grant from the NIH (to A.C.R.), by funds from the ALS Association (A.C.R.), by funds from the Robert H. Lurie Cancer Center (A.C.R.), by a grant from the NIH (to T.V.O.), by a supplement from NIGMS to this same grant (to A.C.R. and T.V.O.), by funds from the ALS Association (T.V.O.), and by an NIH NRSA Training Grant (R.A.P.). The DND-CAT Synchrotron Research Center at the Advanced Photon Sourceis supported by the E.I. Dupont de Nemours & Co., The Dow Chemical Company, the NSF and the State of Illinois.

PY - 1999

Y1 - 1999

N2 - Cellular systems for handling transition metal ions have been identified, but little is known about the structure and function of the specific trafficking proteins. The 1.8 Å resolution structure of the yeast copper chaperone for superoxide dismutase (yCCS) reveals a protein composed of two domains. The N-terminal domain is very similar to the metallochaperone protein Atx1 and is likely to play a role in copper delivery and/or uptake. The second domain resembles the physiological target of yCCS, superoxide dismutase I (SOD1), in overall fold, but lacks all of the structural elements involved in catalysis. In the crystal, two SOD1-like domains interact to form a dimer. The subunit interface is remarkably similar to that in SOD1, suggesting a structural basis for target recognition by this metallochaperone.

AB - Cellular systems for handling transition metal ions have been identified, but little is known about the structure and function of the specific trafficking proteins. The 1.8 Å resolution structure of the yeast copper chaperone for superoxide dismutase (yCCS) reveals a protein composed of two domains. The N-terminal domain is very similar to the metallochaperone protein Atx1 and is likely to play a role in copper delivery and/or uptake. The second domain resembles the physiological target of yCCS, superoxide dismutase I (SOD1), in overall fold, but lacks all of the structural elements involved in catalysis. In the crystal, two SOD1-like domains interact to form a dimer. The subunit interface is remarkably similar to that in SOD1, suggesting a structural basis for target recognition by this metallochaperone.

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Crystal structure of the copper chaperone for superoxide dismutase

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