A thermophilic mini-chaperonin contains a conserved polypeptide-binding surface: Combined crystallographic and NMR studies of the GroEL apical domain with implications for substrate interactions

Journal of Molecular Biology

Volumn 306, Issue 3, 2001, Pages 513-525

  Hua, Qing Xin ^a   Dementieva, Irina S ^b   Walsh, Martin A ^b   Hallenga, Klaas ^a   Weiss, Michael A ^a   Joachimiak, Andrzej ^b  

^a CASE WESTERN RESERVE UNIVERSITY   (United States)

^b ARGONNE NATIONAL LABORATORY   (United States)

Author keywords

Chaperone substrate binding; Crystal structure; NMR spectroscopy; Protein folding; Thermus thermophilus

Indexed keywords

CHAPERONIN; POLYPEPTIDE;

ARTICLE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DIFFRACTION; DNA FOOTPRINTING; ESCHERICHIA COLI; HYDROGEN BOND; MUTAGENESIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN STABILITY; THERMOPHILIC BACTERIUM; THERMUS THERMOPHILUS;

ESCHERICHIA COLI; THERMUS THERMOPHILUS;

EID: 0035936701     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4405     Document Type: Article

References (75)

1. Roles of molecular chaperones in cytoplasmic protein folding
2. Refolding chromatography with immobilized mini chaperones
3. Oxidative refolding chromatography: Folding of the scorpion toxin Cn5
4. Principles that govern the folding of protein chains
5. A mutation in GroEL interferes with protein folding by reducing the rate of discharge of sequestered polypeptides
6. Minimal and optimal mechanisms for GroE-mediated protein folding
7. The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S
8. The crystal structure of the bacterial GroEL at 2.8 Å
9. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
10. A structural model for GroEL-polypeptide recognition
11. The HSP70 and HSP60 chaperone machines
12. Transmissible spongiform encephalopathies, amyloidoses and yeast prions: Common threads?
13. In vivo activities of GroEL minichaperones
14. GroEL recognises sequential and non-sequential linear structural motifs compatible with extended beta-strands and alpha-helices
15. The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity
16. Applications of three- and four-dimensional heteronuclear NMR spectroscopy to protein structure determination
17. Structures of large proteins in solution: Three and four-dimensional heteronuclear NMR spectroscopy
18. Protein misfolding, evolution and disease
19. Proteins as molecular chaperones
20. Principles of protein folding in the cellular environment
21. Interaction of alpha-crystallin with spin-labeled peptides
22. Residues in chaperonin GroEL required for polypeptide binding and release
23. Chaperone-mediated protein folding
24. The Escherichia coli groE chaperonins
25. Thermodynamic stability and folding of GroEL minichaperones
26. 15N-enriched proteins
27. Molecular basis of mammalian determination: Activation of mullerian inhibiting substance gene expression by SRY
28. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis
29. Purification and properties of groE, a host protein involved in bacteriophage assembly
30. Structural aspects of GroEL function
31. Identification of in vivo substrates of the chaperonin GroEL
32. The structure and dynamics of despentapeptide insulin in solution: The molten-globule hypothesis
33. Dynamics of a monomeric insulin analogue: Testing the molten-globule hypothesis
34. Mapping the functional surface of insulin by design: Structure and function of a novel A-chain analogue
35. Nature and consequences of GroEL-protein interactions
36. Capturing the misfolds: Chaperone-peptide-binding motifs
37. Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy
38. NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution
39. Salt bridge stability in monomeric proteins
40. Electrostatic strengths of salt bridges in thermophilic and mesophilic glutamate dehydrogenase monomers
41. The chaperonin GroEL binds a polypeptide in an alpha-helical conformation
42. Different conformations for the same polypeptide bound to chaperones DnaK and GroEL
43. The hydrophobic nature of GroEL-substrate binding
44. Chaperone-assisted protein folding
45. Refinement of macromolecular structures by the maximum likelihood method
46. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
47. Processing of X-ray diffraction data collected in oscillation mode
48. The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
49. Pilus chaperone FimC-adhesin FimH interactions mapped by TROSY-NMR
50. Automated protein model building combined with iteractive structure refinement
51. Chaperonin function: Folding by forced unfolding
52. Unliganded GroEL at 2.8 Å: Structure and functional implication
53. Effects of salt bridges on protein structure and design
54. Immobilization of the C-terminal extension of bovine alphaA-crystallin reduces chaperone-like activity
55. Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
56. N chemical shifts
57. Monomeric chaperonin-60 and its 50-kDa fragment possess the ability to interact with non-native proteins, to suppress aggregation and promote protein folding
58. Identification of substrate binding site of GroEL minichaperone in solution
59. Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering
60. Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis
61. Recognition of distorted DNA structures by HMG domains
62. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
63. Taking MAD to extreme: Ultrafast protein structure determination
64. GroEL-GroES-mediated protein folding requires an intact central cavity
65. Design of highly stable functional GroEL minichaperones
66. Stabilization of GroEL minichaperone by core and surface mutations
67. The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding
68. Thermal unfolding studies of a leucine zipper domain and its specific DNA complex: Implications for scissor's grip recognition
69. Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex
70. 7 chaperonin complex
71. 2H labeled proteins with high sensitivity
72. Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196 → Ala
73. Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
74. Structural analysis of substrate binding by the molecular chaperone DnaK