Conformational change of the E-F interhelical loop in the M photointermediate of bacteriorhodopsin

Journal of Molecular Biology

Volumn 317, Issue 3, 2002, Pages 471-478

  Brown, Leonid S ^a   Needleman, Richard ^b   Lanyi, Janos K ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Bacteriorhodopsin; Cysteine reactivity; Interhelical loop; M intermediate; Protein conformation change

Indexed keywords

BACTERIORHODOPSIN; CYSTEINE; MUTANT PROTEIN; THIOL REAGENT; WATER;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CORRELATION ANALYSIS; CRYSTAL STRUCTURE; EXPOSURE; GENE MUTATION; GENETIC ENGINEERING; HALOBACTERIUM SALINARUM; ILLUMINATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN MOTIF; PROTEIN STRUCTURE; REACTION ANALYSIS; WATER CONTENT;

EID: 0036299067     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2002.5428     Document Type: Article

References (47)

1. The structure and mechanism of the family of retinal proteins from halophilic archaea
2. Progress toward an explicit mechanistic model for the light-driven pump, bacteriorhodopsin
3. Closing in on bacteriorhodopsin: Progress in understanding the molecule
4. Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin
5. Structure of the N intermediate of bacteriorhodopsin revealed by X-ray diffraction
6. Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction
7. Protein conformational changes in the bacteriorhodopsin photocycle
8. Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
9. Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography
10. Coupling photoisomerization of the retinal in bacteriorhodopsin to directional transport
11. Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin
12. Crystal structure of the D85S mutant of bacteriorhodopsin: A model of an O-like photocycle intermediate
13. Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin
14. Spin-labeling studies of the conformational changes in the vicinity of D36, D38, T46, and E161 of bacteriorhodopsin during the photocycle
15. Transient channel-opening in bacteriorhodopsin: An EPR study
16. High-field EPR studies of the structure and conformational changes of site-directed spin labeled bacteriorhodopsin
17. Time-resolved site-directed spin-labeling studies of bacteriorhodopsin: Loop-specific conformational changes in M
18. Unraveling photoexcited conformational changes of bacteriorhodopsin by time resolved electron paramagnetic resonance spectroscopy
19. Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin
20. Light-induced rotation of a transmembrane alpha-helix in bacteriorhodopsin
21. Conformational change of helix G in the bacteriorhodopsin photocycle: Investigation with heavy atom labeling and X-ray diffraction
22. Protonation reactions and their coupling in bacteriorhodopsin
23. Coupling of the reisomerization of the retinal, proton uptake, and reprotonation of asp-96 in the N photointermediate of bacteriorhodopsin
24. Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin Schiff base
25. Effects of hydrostatic pressure on the kinetics reveal a volume increase during the bacteriorhodopsin photocycle
26. Structural changes in bacteriorhodopsin during ion transport at 2 Å resolution
27. Structure of an early intermediate in the M-state phase of the bacteriorhodopsin photocycle
28. Structural features and light-dependent changes in the sequence 59-75 connecting helices I and II in rhodopsin: A site-directed spin-labeling study
29. Single-cysteine substitution mutants at amino acid positions 55-75, the sequence connecting the cytoplasmic ends of helices I and II in rhodopsin: Reactivity of the sulfhydryl groups and their derivatives identifies a tertiary structure that changes upon light-activation
30. Crystal structure of rhodopsin: A G protein-coupled receptor
31. Site-directed spin-labeling reveals the orientation of the amino acid side-chains in the E-F loop of bacteriorhodopsin
32. Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
33. Atomic force microscopy of native purple membrane
34. Structure of bacteriorhodopsin at 1.55 Å resolution
35. Protein, lipid and water organization in bacteriorhodopsin crystals: A molecular view of the purple membrane at 1.9 Å resolution
36. Functional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle
37. Energy coupling in an ion pump. The reprotonation switch of bacteriorhodopsin
38. A local electrostatic change is the cause of the large-scale protein conformation shift in bacteriorhodopsin
39. Partitioning of free energy gain between the photoisomerized retinal and the protein in bacteriorhodopsin
40. Properties of Asp212 → Asn bacteriorhodopsin suggest that Asp212 and Asp85 both participate in a counterion and proton acceptor complex near the Schiff base
41. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
42. Tissue sulfhydryl groups
43. Determination of sulfhydryl groups with 2,2′- or 4,4′-dithiodipyridine
44. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
45. The interpretation of protein structures: Estimation of static accessibility
46. Structural invariants in protein folding
47. The CCP4 suite: Programs for protein crystallography