From Minichaperone to GroEL 1: Information on GroEL-polypeptide interactions from crystal packing of minichaperones

Journal of Molecular Biology

Volumn 304, Issue 5, 2000, Pages 873-881

  Wang, Q ^a   Buckle, A M ^a   Fersht, A R ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Chaperone; Flexibility; Protein folding; Recognition

Indexed keywords

CHAPERONE; CHAPERONIN; POLYPEPTIDE;

ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

EID: 0034671446     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4276     Document Type: Review

References (46)

1. Refolding chromatography with immobilized mini-chaperones
2. Oxidative refolding chromatography: Folding of the scorpion toxin Cn5
3. A polypeptide bound by the chaperonin GroEL is localised within a central cavity
4. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å
5. Model peptide studies demonstrate that amphipathic secondary structures can be recognised by the chaperonin GroEL (Cpn60)
6. The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
7. A structural model for GroEL-polypeptide recognition
8. The CCP4 suite: Programs for protein crystallography
9. In vivo activities of GroEL minichaperones
10. GroEL recognises sequential and non-sequential linear structural motifs compatible with extended beta-strands and alpha-helices
11. From minichaperone to GroEL 2: Importance of avidity of the multisite ring structure
12. The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity
13. Identification of a chaperonin binding site in a chloroplast precursor protein
14. An extensively modified version of MolScript that includes greatly enhanced colouring capabilities
15. Multivalent binding of nonnative substrate proteins by the chaperonin GroEL
16. Residues in chaperonin GroEL required for polypeptide binding and release
17. Identification of in vivo substrates of the chaperonin GroEL
18. Nature and consequences of GroEL-protein interactions
19. Improved methods for building protein models in electron density maps and the location of errors in these models
20. NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution
21. Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space
22. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
23. The chaperonin GroEL binds a polypeptide in an alpha-helical conformation
24. Different conformations for the same polypeptide bound to chaperones DnaK and GroEL
25. Characterization of a functionally important mobile domain of GroES
26. The hydrophobic nature of GroEL-substrate binding
27. Bound substrate polypeptides can generally stabilise the tetradecameric structure of Cpn60 and induce its reassembly from monomers
28. Raster3D version 2.0. A program for photorealistic molecular graphics
29. Refinement of macromolecular structures by the maximum-likelihood method
30. AMoRe: An automated package for molecular replacement
31. Minimal and optimal mechanisms for GroE-mediated protein folding
32. Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL
33. The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
34. Characterisation of a distinct binding site for the prokaryotic chaperone, GroEL, on a human granulocyte ribonuclease
35. RASMOL: Biomolecular graphics for all
36. Chaperonin function: Folding by forced unfolding
37. Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
38. Design of highly stable functional GroEL minichaperones
39. Stabilization of GroEL minichaperones by core and surface mutations
40. Basis of substrate binding by the chaperonin GroEL
41. 7 chaperonin complex
42. Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognises thermally unfolded mature beta-lactamase
43. Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
44. Conformational states bound by the molecular chaperones GroEL and secB: A hidden unfolding (annealing) activity
45. Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB