E W Miles

Summary

Affiliation: National Institutes of Health
Country: USA

Publications

  1. pmc The tryptophan synthase α2β2 complex: a model for substrate channeling, allosteric communication, and pyridoxal phosphate catalysis
    Edith Wilson Miles
    Laboratory of Biochemistry and Genetics, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 288:10084-91. 2013
  2. ncbi request reprint Protein evolution. On the ancestry of barrels
    E W Miles
    NIH, Bethesda, MD 20892 0830, USA
    Science 289:1490. 2000
  3. ncbi request reprint Esmond Emerson Snell (1914-2003)
    Edith Wilson Miles
    Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0830, USA
    J Nutr 134:2907-10. 2004
  4. ncbi request reprint Tryptophan synthase: a multienzyme complex with an intramolecular tunnel
    E W Miles
    Section on Enzyme Structure and Function, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda Maryland 20892 0830, USA
    Chem Rec 1:140-51. 2001
  5. ncbi request reprint Cryocrystallography and microspectrophotometry of a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex reveals allosteric roles of alpha Asp60
    S Rhee
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892, USA
    Biochemistry 37:10653-9. 1998
  6. ncbi request reprint Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes
    S Rhee
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    Biochemistry 36:7664-80. 1997
  7. ncbi request reprint Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (alphaD60N) tryptophan synthase alpha2beta2 complex reveals the correct orientation of active site alphaGlu49
    S Rhee
    Laboratory of Molecular Biology, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 273:8553-5. 1998
  8. ncbi request reprint Exchange of K+ or Cs+ for Na+ induces local and long-range changes in the three-dimensional structure of the tryptophan synthase alpha2beta2 complex
    S Rhee
    Laboratory of Molecular Biology and Laboratory of Biochemical Pharmacology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    Biochemistry 35:4211-21. 1996
  9. ncbi request reprint Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium
    C C Hyde
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892
    J Biol Chem 263:17857-71. 1988
  10. ncbi request reprint The reaction of yeast cystathionine beta-synthase is rate-limited by the conversion of aminoacrylate to cystathionine
    K H Jhee
    Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830, USA
    Biochemistry 40:10873-80. 2001

Collaborators

  • S A Ahmed
  • K D Parris
  • M F Dunn
  • K H Jhee
  • S Rhee
  • D R Davies
  • P McPhie
  • D Ferrari
  • C C Hyde
  • D Niks
  • L H Yang
  • S Takeda
  • K Soda
  • K Hirotsu
  • Y Kawata
  • I Miyahara
  • N Esaki
  • T Yoshimura
  • I Schlichting
  • A Mozzarelli
  • Z Lu
  • A Y Kim
  • K S Anderson
  • X J Yang
  • S Nagata
  • E A Padlan

Detail Information

Publications16

  1. pmc The tryptophan synthase α2β2 complex: a model for substrate channeling, allosteric communication, and pyridoxal phosphate catalysis
    Edith Wilson Miles
    Laboratory of Biochemistry and Genetics, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 288:10084-91. 2013
    ..The structure serves as a model for many other multiprotein complexes that are important for biological processes in prokaryotes and eukaryotes...
  2. ncbi request reprint Protein evolution. On the ancestry of barrels
    E W Miles
    NIH, Bethesda, MD 20892 0830, USA
    Science 289:1490. 2000
    ..who show that this type of protein evolution may also occur in b/a barrel proteins, a common single-domain protein fold. Other single domain proteins may have arisen from similar evolutionary mechanisms...
  3. ncbi request reprint Esmond Emerson Snell (1914-2003)
    Edith Wilson Miles
    Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0830, USA
    J Nutr 134:2907-10. 2004
  4. ncbi request reprint Tryptophan synthase: a multienzyme complex with an intramolecular tunnel
    E W Miles
    Section on Enzyme Structure and Function, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda Maryland 20892 0830, USA
    Chem Rec 1:140-51. 2001
    ..The combined results show that the switching of the enzyme between open and closed conformations couples the catalytic reactions at the alpha and beta active sites and prevents the escape of indole...
  5. ncbi request reprint Cryocrystallography and microspectrophotometry of a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex reveals allosteric roles of alpha Asp60
    S Rhee
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892, USA
    Biochemistry 37:10653-9. 1998
    ..These observations show that alpha Asp60 plays important roles in the closure of loop 6 and in allosteric communication between the alpha- and beta-subunits...
  6. ncbi request reprint Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes
    S Rhee
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    Biochemistry 36:7664-80. 1997
    ..These large-scale changes, the closure of loop 6, and the movements of a small number of side chains in the alpha-beta interaction site provide a structural base for interpreting the allosteric properties of tryptophan synthase...
  7. ncbi request reprint Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (alphaD60N) tryptophan synthase alpha2beta2 complex reveals the correct orientation of active site alphaGlu49
    S Rhee
    Laboratory of Molecular Biology, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 273:8553-5. 1998
    ..Our results demonstrate how cryo-crystallography and mutagenesis can provide insight into enzyme mechanism...
  8. ncbi request reprint Exchange of K+ or Cs+ for Na+ induces local and long-range changes in the three-dimensional structure of the tryptophan synthase alpha2beta2 complex
    S Rhee
    Laboratory of Molecular Biology and Laboratory of Biochemical Pharmacology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    Biochemistry 35:4211-21. 1996
    ..The results provide a structural basis for understanding the effects of cations on activity and intersubunit communication...
  9. ncbi request reprint Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium
    C C Hyde
    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892
    J Biol Chem 263:17857-71. 1988
    ....
  10. ncbi request reprint The reaction of yeast cystathionine beta-synthase is rate-limited by the conversion of aminoacrylate to cystathionine
    K H Jhee
    Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830, USA
    Biochemistry 40:10873-80. 2001
    ..We compare our results with cystathionine beta-synthase with those of related investigations of tryptophan synthase and O-acetylserine sulfhydrylase...
  11. ncbi request reprint Lysine 87 in the beta subunit of tryptophan synthase that forms an internal aldimine with pyridoxal phosphate serves critical roles in transimination, catalysis, and product release
    Z Lu
    Laboratory of Biochemical Pharmacology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892
    J Biol Chem 268:8727-34. 1993
    ....
  12. ncbi request reprint Yeast cystathionine beta-synthase is a pyridoxal phosphate enzyme but, unlike the human enzyme, is not a heme protein
    K H Jhee
    Laboratory of Biochemistry and Genetics, NIDDK, National Institutes of Health, Bethesda, Maryland 20892 0830, USA
    J Biol Chem 275:11541-4. 2000
    ..The results are consistent with the absence of heme in the closely related enzymes O-acetylserine sulfhydrylase, threonine deaminase, and tryptophan synthase...
  13. ncbi request reprint The tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography and mutagenesis
    C C Hyde
    Laboratory of Molecular Biology, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892
    Biotechnology (N Y) 8:27-32. 1990
    ..Recombinant DNA technology should also be useful in analyzing protein-protein interaction, protein folding and the channeling phenomenon...
  14. ncbi request reprint Beta D305A mutant of tryptophan synthase shows strongly perturbed allosteric regulation and substrate specificity
    D Ferrari
    Department of Biochemistry, University of California at Riverside, 92521, USA
    Biochemistry 40:7421-32. 2001
    ..This work establishes important roles for betaAsp 305 both in the conformational change between open and closed states that takes place at the beta-site during the formation of the E(A-A) and in substrate binding and recognition...
  15. ncbi request reprint Stereochemistry of the transamination reaction catalyzed by aminodeoxychorismate lyase from Escherichia coli: close relationship between fold type and stereochemistry
    K H Jhee
    Institute for Chemical Research, Kyoto University, Gokasho, Uji, Kyoto, 611 0011, Japan
    J Biochem 128:679-86. 2000
    ..Mizutani, H., Miyahara, I., Hirotsu, K., Takeda, S., Jhee, K.-H., Yoshimura, T., and Esaki, N. (2000) J. Biochem. 128, 29-38]...
  16. ncbi request reprint Structural and kinetic analysis of a channel-impaired mutant of tryptophan synthase
    I Schlichting
    Max Planck Institut fur medizinische Forschung, Abteilung Biophysik, Heidelberg, Federal Republic of Germany
    J Biol Chem 269:26591-3. 1994
    ....