P B Sigler

Summary

Affiliation: Yale University
Country: USA

Publications

  1. ncbi request reprint Structure and function in GroEL-mediated protein folding
    P B Sigler
    Department of Molecular Biophysics and Biochemistry, School of Medicine, Yale University, New Haven, Connecticut 06510, USA
    Annu Rev Biochem 67:581-608. 1998
  2. pmc The 2.1-A crystal structure of an archaeal preinitiation complex: TATA-box-binding protein/transcription factor (II)B core/TATA-box
    P F Kosa
    Department of Molecular Biophysics and Biochemistry, and the Howard Hughes Medical Institute, Yale University, 260 Whitney Avenue, JWG 423, New Haven CT 06511, USA
    Proc Natl Acad Sci U S A 94:6042-7. 1997
  3. ncbi request reprint Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
    H S Rye
    Howard Hughes Medical Institute, Department of Genetics, School of Medicine, Yale University, New Haven, Connecticut 06510, USA
    Nature 388:792-8. 1997
  4. ncbi request reprint The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    Z Xu
    The Howard Hughes Medical Institute, The Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510, USA
    Nature 388:741-50. 1997
  5. ncbi request reprint The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S
    J P Noel
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510
    Nature 366:654-63. 1993
  6. ncbi request reprint Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation
    M Han
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA
    Structure 9:869-80. 2001
  7. ncbi request reprint Crystal structure of the yeast TFIIA/TBP/DNA complex
    J H Geiger
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06510, USA
    Science 272:830-6. 1996
  8. ncbi request reprint Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus
    Y Wang
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511, USA
    Nat Struct Biol 4:650-6. 1997
  9. ncbi request reprint The crystal structure of a hyperthermophilic archaeal TATA-box binding protein
    B S DeDecker
    Department of Molecular Biophysics and Biochemistry and the Howard Hughes Medical Institute, Yale University, New Haven, CT 06511 8114, USA
    J Mol Biol 264:1072-84. 1996
  10. ncbi request reprint Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein
    D G Lambright
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510
    Nature 369:621-8. 1994

Collaborators

Detail Information

Publications44

  1. ncbi request reprint Structure and function in GroEL-mediated protein folding
    P B Sigler
    Department of Molecular Biophysics and Biochemistry, School of Medicine, Yale University, New Haven, Connecticut 06510, USA
    Annu Rev Biochem 67:581-608. 1998
    ..This process allows the polypeptide to achieve its final native state, if folding was completed, or to recycle to another chaperonin molecule, if the folding process did not result in a form committed to the native state...
  2. pmc The 2.1-A crystal structure of an archaeal preinitiation complex: TATA-box-binding protein/transcription factor (II)B core/TATA-box
    P F Kosa
    Department of Molecular Biophysics and Biochemistry, and the Howard Hughes Medical Institute, Yale University, 260 Whitney Avenue, JWG 423, New Haven CT 06511, USA
    Proc Natl Acad Sci U S A 94:6042-7. 1997
    ....
  3. ncbi request reprint Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
    H S Rye
    Howard Hughes Medical Institute, Department of Genetics, School of Medicine, Yale University, New Haven, Connecticut 06510, USA
    Nature 388:792-8. 1997
    ..These observations offer an explanation of why GroEL functions as a double-ring complex...
  4. ncbi request reprint The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    Z Xu
    The Howard Hughes Medical Institute, The Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510, USA
    Nature 388:741-50. 1997
    ..When combined with new functional results, this negative allosteric mechanism suggests a model for an ATP-driven folding cycle that requires a double toroid...
  5. ncbi request reprint The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S
    J P Noel
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510
    Nature 366:654-63. 1993
    ....
  6. ncbi request reprint Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation
    M Han
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA
    Structure 9:869-80. 2001
    ..They compete with G proteins for binding to activated phosphorylated receptors, initiate receptor internalization, and activate additional signaling pathways...
  7. ncbi request reprint Crystal structure of the yeast TFIIA/TBP/DNA complex
    J H Geiger
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06510, USA
    Science 272:830-6. 1996
    ..The four-helix-bundle domain projects away from the TBP/TATA complex, thereby presenting a substantial surface for further protein-protein interactions...
  8. ncbi request reprint Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus
    Y Wang
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511, USA
    Nat Struct Biol 4:650-6. 1997
    ..The exchange mechanism may have useful implications for receptor-induced exchange in heterotrimeric G proteins...
  9. ncbi request reprint The crystal structure of a hyperthermophilic archaeal TATA-box binding protein
    B S DeDecker
    Department of Molecular Biophysics and Biochemistry and the Howard Hughes Medical Institute, Yale University, New Haven, CT 06511 8114, USA
    J Mol Biol 264:1072-84. 1996
    ..The total reliance on a hydrophobic interface with DNA may explain the enhanced affinity of PwTBP for its DNA promoter at higher temperatures and increased salt concentration...
  10. ncbi request reprint Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein
    D G Lambright
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510
    Nature 369:621-8. 1994
    ..The changes are distinct from those observed in other members of the GTPase superfamily...
  11. ncbi request reprint The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S
    D C Boisvert
    Department of Genetics, Yale University School of Medicine, New Haven, Connecticut 06510, USA
    Nat Struct Biol 3:170-7. 1996
    ..Although bound ATP induces modest conformational shifts in the equatorial domain, the stereochemistry that functionally coordinates GroEL's affinity for nucleotides, polypeptide, and GroES remains uncertain...
  12. ncbi request reprint DNA-binding mechanism of the monomeric orphan nuclear receptor NGFI-B
    G Meinke
    Department of Molecular Biophysics and Biochemistry and the Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06511, USA
    Nat Struct Biol 6:471-7. 1999
    ....
  13. ncbi request reprint The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity
    L Chen
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511, USA
    Cell 99:757-68. 1999
    ..Our structural analysis, combined with other results, suggests that various modes of molecular plasticity are responsible for tight promiscuous binding of nonnative substrates and their release into the shielded cis assembly...
  14. pmc The structural basis for the oriented assembly of a TBP/TFB/promoter complex
    O Littlefield
    Department of Molecular Biophysics, Yale University, New Haven CT 06511, USA
    Proc Natl Acad Sci U S A 96:13668-73. 1999
    ..This interaction is important in determining the level of basal transcription and explicitly defines the direction of transcription...
  15. ncbi request reprint Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    K M Ferguson
    Department of Chemistry, Yale University, New Haven, Connecticut 06510, USA
    Cell 83:1037-46. 1995
    ..Using electrostatics and varying levels of head-group specificity, PH domains may localize and orient signaling proteins, providing a general membrane targeting and regulatory function...
  16. ncbi request reprint Crystal structure of a yeast TBP/TATA-box complex
    Y Kim
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510
    Nature 365:512-20. 1993
    ..The severe bend and a positive writhe radically alter the trajectory of the flanking B-form DNA...
  17. ncbi request reprint Atomic structure of progesterone complexed with its receptor
    S P Williams
    Department of Molecular Biophysics and Biochemistry, and the Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06510, USA
    Nature 393:392-6. 1998
    ..The structure also indicates that the analogous 3-keto-steroid receptors may have a similar mechanism of action...
  18. ncbi request reprint Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A
    K C Slep
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511, USA
    Nature 409:1071-7. 2001
    ..Effector binding to a nucleotide-dependent site on alpha(t) sequesters PDEgamma residues implicated in PDE inhibition, and potentiates recruitment of RGS9 for hydrolytic transition state stabilization and concomitant signal termination...
  19. ncbi request reprint Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli
    G D Van Duyne
    Department of Molecular Biochemistry and Biophysics, Howard Hughes Medical Institute, Yale University, New Haven, CT 06510 USA
    J Mol Biol 256:377-91. 1996
    ....
  20. ncbi request reprint Sst2 is a GTPase-activating protein for Gpa1: purification and characterization of a cognate RGS-Galpha protein pair in yeast
    D M Apanovitch
    Department of Pharmacology and Molecular Cardiobiology Program, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, Connecticut 06536, USA
    Biochemistry 37:4815-22. 1998
    ..These experiments represent the first biochemical characterization of Gpa1 and Sst2, and provide a molecular basis for their well-established biological roles in signaling and desensitization...
  21. ncbi request reprint Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue
    D L Scott
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511
    Science 250:1563-6. 1990
    ..Comparison of the bee-venom enzyme with other phospholipase structures provides compelling evidence for a common catalytic mechanism...
  22. ncbi request reprint Crystal structure of a G-protein beta gamma dimer at 2.1A resolution
    J Sondek
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510, USA
    Nature 379:369-74. 1996
    ..The structure details interactions between G protein beta- and gamma-subunits and highlights regions implicated in effector modulation for the conserved family of G protein beta gamma dimers...
  23. ncbi request reprint A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G proteins by phosducin
    R Gaudet
    Department of Molecular Biophysics, Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06511, USA
    Mol Cell 3:649-60. 1999
    ..This transition disrupts phosducin's interface with Gt beta gamma, leading to the release of unencumbered Gt beta gamma, which reassociates with the membrane and Gt alpha to form a signaling-competent Gt alpha beta gamma heterotrimer...
  24. ncbi request reprint Structural determinants of nuclear receptor assembly on DNA direct repeats
    F Rastinejad
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510, USA
    Nature 375:203-11. 1995
    ..The stereochemistry suggests a mechanism by which heterodimers recognize the inter-half-site spacing between direct repeats...
  25. pmc Structural basis of preinitiation complex assembly on human pol II promoters
    F T Tsai
    Department of Molecular Biophysics and Biochemistry and the Howard Hughes Medical Institute, Yale University, New Haven, CT 06511, USA
    EMBO J 19:25-36. 2000
    ..Binding of TFIIBc is, therefore, synergistic with TBPc requiring the distortion of the TATA-box. Thus, the newly described TFIIBc-DNA interface is likely to be a key determinant for the unidirectional assembly of a functional PIC...
  26. ncbi request reprint Activating mineralocorticoid receptor mutation in hypertension exacerbated by pregnancy
    D S Geller
    Howard Hughes Medical Institute, Department of Genetics, Yale University School of Medicine, Boyer Center for Molecular Medicine, Room 154, 295 Congress Avenue, New Haven, CT 06510, USA
    Science 289:119-23. 2000
    ..This helix 5-helix 3 interaction is highly conserved among diverse nuclear hormone receptors, suggesting its general role in receptor activation...
  27. ncbi request reprint Structure and importance of the dimerization domain in elongation factor Ts from Thermus thermophilus
    Y Jiang
    Department of Chemistry, Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06520, USA
    Biochemistry 35:10269-78. 1996
    ..Surprisingly, EF-Ts monomers created in this manner failed to catalyze nucleotide exchange in EF-Tu, indicating that, in vitro. T. thermophilus EF-Ts functions only as a homodimer...
  28. ncbi request reprint The crystal structure of the bacterial chaperonin GroEL at 2.8 A
    K Braig
    Department of Genetics, Yale University School of Medicine, Boyer Center, New Haven, Connecticut 06510
    Nature 371:578-86. 1994
    ..The three-dimensional structure places most of the mutationally defined functional sites on the channel walls and its outward invaginations, and at the ends of the cylinder...
  29. pmc Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains
    D M Tanenbaum
    Department of Molecular Biophysics and Biochemistry and the Howard Hughes Medical Institute, Yale University, 260 Whitney Avenue, JWG 423, New Haven, CT 06511, USA
    Proc Natl Acad Sci U S A 95:5998-6003. 1998
    ..A peculiar crystal packing event displaces helix 12 in the hERalphaLBD reported here, suggesting a higher degree of dynamic variability than expected for this critical substructure...
  30. ncbi request reprint Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin
    K M Ferguson
    Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06510
    Cell 79:199-209. 1994
    ..This surface includes the position of the X-linked immunodeficiency mutation in the Btk PH domain and may serve as a ligand-binding surface...
  31. ncbi request reprint The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation
    J A Hirsch
    Howard Hughes Medical Institute, Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511, USA
    Cell 97:257-69. 1999
    ..In conjunction with biochemical and mutagenesis data, we propose a molecular mechanism by which arrestin is activated for receptor binding...
  32. ncbi request reprint Structure of NF-kappa B p50 homodimer bound to a kappa B site
    G Ghosh
    Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06510
    Nature 373:303-10. 1995
    ..The carboxy-terminal domains form a dimerization interface between beta-sheets using residues that are strongly conserved in the Rel family...
  33. ncbi request reprint GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4
    J Sondek
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut
    Nature 372:276-9. 1994
    ..GTP gamma S, but also conserved residues for GTPase activity. Thus the Gt alpha.GDP.AIF-4.H2O structure provides new insight into the mechanism of GTP hydrolysis...
  34. ncbi request reprint Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate
    D L Scott
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511
    Science 254:1007-10. 1991
    ....
  35. ncbi request reprint The stereochemistry and biochemistry of the trp repressor-operator complex
    B F Luisi
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 66511
    Biochim Biophys Acta 1048:113-26. 1990
  36. ncbi request reprint Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA
    B F Luisi
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511
    Nature 352:497-505. 1991
    ..The DNA-induced dimer fixes the separation of the subunits' recognition surfaces so that the spacing between the half-sites becomes a critical feature of the target sequence's identity...
  37. pmc Purification and characterization of trp aporepressor
    A Joachimiak
    Proc Natl Acad Sci U S A 80:668-72. 1983
    ..Preliminary equilibrium dialysis experiments suggest that tryptophan binds to the aporepressor with a dissociation constant of 1.6 X 10(-5) M...
  38. ncbi request reprint The three-dimensional structure of trp repressor
    R W Schevitz
    Nature 317:782-6. 1985
    ..The binding of L-tryptophan activates the aporepressor indirectly by fixing the orientation of the second helix of the helix-turn-helix motif and by moulding the details of the repressor's structure near the DNA binding surface...
  39. ncbi request reprint The crystal structure of trp aporepressor at 1.8 A shows how binding tryptophan enhances DNA affinity
    R G Zhang
    Nature 327:591-7. 1987
    ..These flexible 'DNA-reading heads' flank a highly inflexible core domain formed by an unusual arrangement of interlocking alpha-helices from both subunits...
  40. pmc The DNA target of the trp repressor
    T E Haran
    Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511
    EMBO J 11:3021-30. 1992
    ....
  41. ncbi request reprint The structure of trp pseudorepressor at 1.65A shows why indole propionate acts as a trp 'inducer'
    C L Lawson
    Department of Biochemistry and Molecular Biology, University of Chicago, Illinois 60637
    Nature 333:869-71. 1988
    ..This explains why IPA acts as an apparent trp inducer...
  42. ncbi request reprint Crystal structure of trp repressor/operator complex at atomic resolution
    Z Otwinowski
    Department of Biochemistry and Molecular Biology, University of Chicago, Illinois 60637
    Nature 335:321-9. 1988
    ..Water-mediated polar contacts to the bases also appear to contribute part of the specificity...
  43. ncbi request reprint Flexibility of the DNA-binding domains of trp repressor
    C L Lawson
    Department of Biochemistry and Molecular Biology, University of Chicago, Illinois 60637
    Proteins 3:18-31. 1988
    ..This flexibility may be required by the various binding modes proposed for trp repressor in its search for and adherence to its three different operator sites...
  44. ncbi request reprint Functional inferences from crystals of Escherichia coli trp repressor
    A Joachimiak
    J Biol Chem 258:12641-3. 1983
    ....