ATP-bound states of GroEL captured by cryo-electron microscopy

Cell

Volumn 107, Issue 7, 2001, Pages 869-879

  Ranson, Neil A ^a   Farr, George W ^b,c   Roseman, Alan M ^a   Gowen, Brent ^d   Fenton, Wayne A ^c   Horwich, Arthur L ^b,c   Saibil, Helen R ^a  

^a UNIVERSITY OF LONDON   (United Kingdom)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^c YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CHAPERONIN; POLYPEPTIDE; PROTEIN SUBUNIT;

ARTICLE; BINDING AFFINITY; BINDING SITE; CRYOELECTRON MICROSCOPY; ENZYME BINDING; ENZYME SUBSTRATE COMPLEX; MOLECULAR INTERACTION; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE;

EID: 0035966323     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(01)00617-1     Document Type: Article

References (46)

1. The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPgS
2. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
3. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å
4. The Hsp70 and Hsp60 chaperone machines
5. The origins and consequences of asymmetry in the chaperonin reaction cycle
6. Release of both native and non-native proteins from a cis-only GroEL ternary complex
7. Purification and properties of the groES morphogenetic protein of Escherichia coli
8. Folding of malate dehydrogenase inside the GroEL-GroES cavity
9. A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL
10. Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
11. MRC image processing programs
12. Cryo-electron microscopy of vitrified specimens
13. An extensively modified version of Molscript that includes greatly enhanced coloring capabilities
14. Multivalent binding of non-native substrate proteins by the chaperonin GroEL
15. Residues in chaperonin GroEL required for polypeptide binding and release
16. SPIDER and WEB; processing and visualization of images in 3D electron microscopy and related fields
17. Cooperativity in ATP hydrolysis by GroEL is increased by GroES
18. Molecular chaperones in cellular protein folding
19. Binding and hydrolysis of nucleotide1s in the chaperonin catalytic cycle: Implications for the mechanism of assisted protein folding
20. Improved methods for building models in electron density maps and the location of errors in these models
21. Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings
22. Escherichia coli aspartate transcarbamoylase: The molecular basis for a concerted allosteric transition
23. Molscript - A program to produce both detailed and schematic plots of protein structures
24. A dynamic model for the allosteric mechanism of GroEL
25. Protein folding in the central cavity of the GroEL-GroES chaperonin complex
26. Raster3d version-2.0 - A program for photorealistic molecular graphics
27. Chaperonins
28. Docking structures of domains into maps from cryo-electron microscopy using local correlation
29. The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
30. The ATP-bound state of the E. coli chaperonin GroEL studied by cryo-electron microscopy
31. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
32. GroEL-GroES cycling: ATP and non-native polypeptide direct alternation of folding active rings
33. Chaperonin function: Folding by forced unfolding
34. Structure and function in GroEL-mediated protein folding
35. Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and GroES
36. Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
37. A new generation of the IMAGIC image processing system
38. Energy transduction in the F1 motor of ATP synthase
39. Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under GroES
40. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction
41. Structural basis of allosteric changes in the GroEL mutant Arg197→Ala
42. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
43. Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196→Ala
44. Nested co-operativity in the ATPase activity of the oligomeric chaperonin GroEL
45. Mapping the transition state of the allosteric pathway of GroEL by protein engineering
46. Transient kinetic analysis of adenosine 5′-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL