A C Rosenzweig

Summary

Affiliation: Northwestern University
Country: USA

Publications

  1. ncbi request reprint Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution
    A C Rosenzweig
    Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA
    Structure 7:605-17. 1999
  2. ncbi request reprint Structure and chemistry of the copper chaperone proteins
    A C Rosenzweig
    Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA
    Curr Opin Chem Biol 4:140-7. 2000
  3. ncbi request reprint Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
    A L Lamb
    Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA
    Nat Struct Biol 8:751-5. 2001
  4. ncbi request reprint Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins
    A K Wernimont
    Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA
    Nat Struct Biol 7:766-71. 2000
  5. ncbi request reprint Heterodimer formation between superoxide dismutase and its copper chaperone
    A L Lamb
    Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA
    Biochemistry 39:14720-7. 2000
  6. ncbi request reprint Crystal structure of the second domain of the human copper chaperone for superoxide dismutase
    A L Lamb
    Department of Biochemistry, Molecular Biology, and Cell Biology and Department of Chemistry, Northwestern University, Evanston, Illinois 60208, USA
    Biochemistry 39:1589-95. 2000
  7. ncbi request reprint Crystal structure of the copper chaperone for superoxide dismutase
    A L Lamb
    1 Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois, 60208, USA
    Nat Struct Biol 6:724-9. 1999
  8. ncbi request reprint Crystal structure of a novel red copper protein from Nitrosomonas europaea
    R L Lieberman
    Departments of Biochemistry, Molecular Biology, and Cell Biology and of Chemistry, Northwestern University, Evanston, Illinois 60208, USA
    Biochemistry 40:5674-81. 2001
  9. ncbi request reprint Structure of beta-lactam synthetase reveals how to synthesize antibiotics instead of asparagine
    M T Miller
    Department of Biochemistry, Northwestern University, Evanston, Illinois 60208, USA
    Nat Struct Biol 8:684-9. 2001
  10. ncbi request reprint Copper delivery by metallochaperone proteins
    A C Rosenzweig
    Departments of Biochemistry, Molecular Biology, and Cell Biology and of Chemistry, Northwestern University, Evanston, Illinois 60208, USA
    Acc Chem Res 34:119-28. 2001

Collaborators

  • D L Huffman
  • J Stubbe
  • V C Culotta
  • A L Lamb
  • T V O'Halloran
  • W C Voegtli
  • A K Wernimont
  • R L Lieberman
  • M T Miller
  • A S Torres
  • R A Pufahl
  • J Ge
  • A B Hooper
  • D L Perlstein
  • B O Bachmann
  • C A Townsend
  • D M Arciero
  • F Rusnak
  • N J Reiter
  • D J White

Detail Information

Publications12

  1. ncbi request reprint Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution
    A C Rosenzweig
    Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA
    Structure 7:605-17. 1999
    ....
  2. ncbi request reprint Structure and chemistry of the copper chaperone proteins
    A C Rosenzweig
    Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA
    Curr Opin Chem Biol 4:140-7. 2000
    ..In addition, biochemical studies of CCS suggested that chaperones are required in vivo because intracellular copper concentrations are extremely low and also indicated that copper transfer occurs via a direct protein-protein interaction...
  3. ncbi request reprint Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
    A L Lamb
    Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA
    Nat Struct Biol 8:751-5. 2001
    ..This domain is linked to SOD1 by an intermolecular disulfide bond that may facilitate or regulate copper delivery...
  4. ncbi request reprint Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins
    A K Wernimont
    Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA
    Nat Struct Biol 7:766-71. 2000
    ..Taken together, the structures provide models for intermediates in metal ion transfer and suggest a detailed molecular mechanism for protein recognition and metal ion exchange between MT/HCXXC containing domains...
  5. ncbi request reprint Heterodimer formation between superoxide dismutase and its copper chaperone
    A L Lamb
    Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA
    Biochemistry 39:14720-7. 2000
    ..These findings, taken together with structural, biochemical, and genetic studies, strongly suggest that in vivo copper loading of yeast SOD1 occurs via a heterodimeric intermediate...
  6. ncbi request reprint Crystal structure of the second domain of the human copper chaperone for superoxide dismutase
    A L Lamb
    Department of Biochemistry, Molecular Biology, and Cell Biology and Department of Chemistry, Northwestern University, Evanston, Illinois 60208, USA
    Biochemistry 39:1589-95. 2000
    ..In contrast to SOD1, however, the hCCS structure does not contain a copper ion bound in the catalytic site. Notably, the structure reveals a single loop proximal to the dimer interface which is unique to the CCS chaperones...
  7. ncbi request reprint Crystal structure of the copper chaperone for superoxide dismutase
    A L Lamb
    1 Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois, 60208, USA
    Nat Struct Biol 6:724-9. 1999
    ..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...
  8. ncbi request reprint Crystal structure of a novel red copper protein from Nitrosomonas europaea
    R L Lieberman
    Departments of Biochemistry, Molecular Biology, and Cell Biology and of Chemistry, Northwestern University, Evanston, Illinois 60208, USA
    Biochemistry 40:5674-81. 2001
    ..Moreover, the red copper center is square pyramidal whereas blue copper is typically distorted tetrahedral. Analysis of the NC structure provides insight into possible functions of this new type of biological copper center...
  9. ncbi request reprint Structure of beta-lactam synthetase reveals how to synthesize antibiotics instead of asparagine
    M T Miller
    Department of Biochemistry, Northwestern University, Evanston, Illinois 60208, USA
    Nat Struct Biol 8:684-9. 2001
    ..The structural data provide the opportunity to alter the synthetic potential of beta-LS, perhaps leading to the creation of new beta-lactamase inhibitors and beta-lactam antibiotics...
  10. ncbi request reprint Copper delivery by metallochaperone proteins
    A C Rosenzweig
    Departments of Biochemistry, Molecular Biology, and Cell Biology and of Chemistry, Northwestern University, Evanston, Illinois 60208, USA
    Acc Chem Res 34:119-28. 2001
    ..Crystallographic studies of these two copper chaperone families have provided insights into metal binding and target recognition by metallochaperones and have led to detailed molecular models for the copper transfer mechanism...
  11. pmc Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer
    W C Voegtli
    Department of Biochemistry, Northwestern University, Evanston, IL 60208, USA
    Proc Natl Acad Sci U S A 98:10073-8. 2001
    ..No metal-binding site is observed in Y4. Instead, the residues in the active site region form a hydrogen-bonding network involving an arginine, two glutamic acids, and a water molecule...
  12. ncbi request reprint Structure of the bacteriophage lambda Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes
    W C Voegtli
    Department of Biochemistry, Northwestern University, Evanston, Illinois 60208, USA
    Biochemistry 39:15365-74. 2000
    ..The two different active site structures provide models for intermediates in phosphoester hydrolysis and suggest specific mechanistic roles for conserved residues...