Structure of the molecular chaperone prefoldin: Unique interaction of multiple coiled coil tentacles with unfolded proteins

Cell

Volumn 103, Issue 4, 2000, Pages 621-632

  Siegert, Ralf ^a   Leroux, Michel R ^a   Scheufler, Clemens ^a   Hartl, F Ulrich ^a   Moarefi, Ismail ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHAPERONIN; PREFOLDIN; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; GEL PERMEATION CHROMATOGRAPHY; METHANOBACTERIUM THERMOAUTOTROPHICUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE;

ARCHAEA; EUKARYOTA; METHANOBACTERIUM; METHANOTHERMOBACTER THERMAUTOTROPHICUS;

EID: 0033680802     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)00165-3     Document Type: Article

References (63)

1. Interaction of Hsp70 with newly-synthesized proteins: Implications for protein folding and assembly
2. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å
3. Crystallography and NMR system: A new software suite for macromolecular structure determination
4. The Hsp70 and Hsp60 chaperone machines
5. Ribbons
6. The CCP4 Suite - Programs for protein crystallography
7. The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity
8. Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy
9. GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism
10. The packing of α-helices: Simple coiled coils
11. Trigger factor and DnaK cooperate in folding of newly synthesized proteins
12. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
13. Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells
14. Principles of protein folding in the cellular environment
15. In vivo observation of polypeptide flux through the bacterial chaperonin system
16. Residues in chaperonin GroEL required for polypeptide binding and release
17. Chaperone-mediated protein folding
18. Function in protein folding of TRIC, a cytosolic ring complex containing TCP-1 and structurally related subunits
19. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
20. A cytoplasmic chaperonin that catalyzes beta-actin folding
21. A novel protein complex promoting formation of functional alpha- and gammatubulin
22. Discontinuous occurrence of the hsp70 (dnaK) gene among Archaea and sequence features of HSP70 suggest a novel outlook on phylogenies inferred from this protein
23. Group II chaperonins: New TRIC(k)s and turns of a protein folding machine
24. Prefoldinnascent chain complexes in the folding of cytoskeletal proteins
25. Molecular chaperones in cellular protein folding
26. Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding
27. Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
28. Identification of in vivo substrates of the chaperonin GroEL
29. Improved methods for building protein models in electron-density maps and the location of errors in these models
30. Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains
31. Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin
32. NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution
33. Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
34. The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol
35. Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accomodates the protein substrate within its central cavity
36. MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin
37. Protein folding: Versatility of the cytosolic chaperonin TRiC/CCT
38. 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin
39. Coiled coils: New structures and new functions
40. Protein folding in the central cavity of the GroEL-GroES chaperonin complex
41. The accessible surface area and stability of oligomeric proteins
42. The translation machinery and 70 kd heat shock protein cooperate in protein synthesis
43. Grasp - Graphical representation and analysis of surface-properties
44. Processing of X-ray diffraction data collected in oscillation mode
45. Automated protein model building combined with iterative structure refinement
46. The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
47. Hydrophobicity of polar amino acid side chains is markedly reduced by flanking peptide bonds
48. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
49. Molecular chaperones: Containers and surfaces for folding, stabilising or unfolding proteins
50. Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
51. Three conformations of an archaeal chaperonin, TF55 from Sulfolobus shibatae
52. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
53. Chaperonin function: Folding by forced unfolding
54. Compartmentation of protein folding in vivo: Sequestration of non-native polypeptide by the chaperonin-GimC system
55. Structure and function in GroEL-mediated protein folding
56. Automated MAD and MIR structure solution
57. Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains
58. In vivo newly translated polypeptides are sequestered in a protected folding environment
59. Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin
60. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction
61. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
62. TCP1 complex is a molecular chaperone in tubulin biogenesis
63. Structural analysis of substrate binding by the molecular chaperone DnaK