E B Fauman

Summary

Affiliation: University of Michigan
Country: USA

Publications

  1. ncbi Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A
    E B Fauman
    Department of Biological Chemistry, The University of Michigan, Ann Arbor 48109 1055, USA
    Cell 93:617-25. 1998
  2. ncbi The X-ray crystal structures of Yersinia tyrosine phosphatase with bound tungstate and nitrate. Mechanistic implications
    E B Fauman
    Biophysics Research Division and the Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109 1055, USA
    J Biol Chem 271:18780-8. 1996
  3. ncbi A ligand-induced conformational change in the Yersinia protein tyrosine phosphatase
    H L Schubert
    Biophysics Research Division, University of Michigan, Ann Arbor 48109 1055, USA
    Protein Sci 4:1904-13. 1995
  4. ncbi Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate
    J A Stuckey
    Department of Biological Chemistry, University of Michigan, Ann Arbor 48109 1055
    Nature 370:571-5. 1994
  5. ncbi Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases
    K M Perry
    Department of Biochemistry and Biophysics, University of California, San Francisco 94143 0448
    Proteins 8:315-33. 1990
  6. ncbi Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and an anti-folate
    W R Montfort
    Department of Biochemistry and Biophysics, University of California, San Francisco 94143 0448
    Biochemistry 29:6964-77. 1990
  7. ncbi Water-mediated substrate/product discrimination: the product complex of thymidylate synthase at 1.83 A
    E B Fauman
    Department of Biochemistry and Biophysics, University of California, San Francisco 94143 0448
    Biochemistry 33:1502-11. 1994
  8. ncbi RNA methylation under heat shock control
    H Bugl
    Department of Biology, University of Michigan, Ann Arbor 48109, USA
    Mol Cell 6:349-60. 2000

Collaborators

  • Robert Stroud
  • U Jakob
  • Zhong Yin Zhang
  • H Bugl
  • M A Saper
  • H L Schubert
  • J A Stuckey
  • J C Bardwell
  • B L Staker
  • F Zheng
  • S R Kushner
  • J E Dixon
  • W R Montfort
  • K M Perry
  • G F Maley
  • F Maley
  • J S Finer-Moore
  • L Hardy

Detail Information

Publications8

  1. ncbi Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A
    E B Fauman
    Department of Biological Chemistry, The University of Michigan, Ann Arbor 48109 1055, USA
    Cell 93:617-25. 1998
    ..We propose that Glu-431 may act as a general acid. Structure-based alignments suggest that the noncatalytic domain of the MAP kinase phosphatases will share this topology, as will ACR2, a eukaryotic arsenical resistance protein...
  2. ncbi The X-ray crystal structures of Yersinia tyrosine phosphatase with bound tungstate and nitrate. Mechanistic implications
    E B Fauman
    Biophysics Research Division and the Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109 1055, USA
    J Biol Chem 271:18780-8. 1996
    ..Since nearly all of the 47 invariant or highly conserved residues of the PTPase domain are clustered at the active site, we suggest that the mechanism postulated for the Yersinia enzyme is applicable to all the PTPases...
  3. ncbi A ligand-induced conformational change in the Yersinia protein tyrosine phosphatase
    H L Schubert
    Biophysics Research Division, University of Michigan, Ann Arbor 48109 1055, USA
    Protein Sci 4:1904-13. 1995
    ..We speculate that the intrinsic loop flexibility of different PTPases may be related to their catalytic rate and may play a role in the wide range of activities observed within this enzyme family...
  4. ncbi Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate
    J A Stuckey
    Department of Biological Chemistry, University of Michigan, Ann Arbor 48109 1055
    Nature 370:571-5. 1994
    ..The same anion-binding loop in PTPases is also found in the enzyme rhodanese...
  5. ncbi Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases
    K M Perry
    Department of Biochemistry and Biophysics, University of California, San Francisco 94143 0448
    Proteins 8:315-33. 1990
    ..0 A from the substitution. This represents the plastic accommodation of the protein which is parameterized in terms of thermal B factor and distance from a mutational change...
  6. ncbi Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and an anti-folate
    W R Montfort
    Department of Biochemistry and Biophysics, University of California, San Francisco 94143 0448
    Biochemistry 29:6964-77. 1990
    ..The ligand-induced conformational change is not a domain shift but involves the segmental accommodation of several helices, beta-strands, and loops that move as units against the beta-sheet interface between monomers...
  7. ncbi Water-mediated substrate/product discrimination: the product complex of thymidylate synthase at 1.83 A
    E B Fauman
    Department of Biochemistry and Biophysics, University of California, San Francisco 94143 0448
    Biochemistry 33:1502-11. 1994
    ....
  8. ncbi RNA methylation under heat shock control
    H Bugl
    Department of Biology, University of Michigan, Ann Arbor 48109, USA
    Mol Cell 6:349-60. 2000
    ..Null mutations in ftsJ show a dramatically altered ribosome profile, a severe growth disadvantage, and a temperature-sensitive phenotype. Our results reveal an unexpected link between the heat shock response and RNA metabolism...