Motion in Bacteriorhodopsin (bR) [br]

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Classification Suspected Fragment Motion, Shear Mechanism [F-s-2]

Structures 1BRD Conformation 1 [ PartsList ] 2BRD Conformation 1 [ PartsList ]

Description This is a seven-helix transmembrane protein. In one intermediate in this cycle (M), movement is suspected in two helices (F and G). The seven transmembrane helices are packed around a chromophore. Light interacting with the chromophore drives the protein through a photocycle that pumps protons across the membrane. The major conformational changes in the photocycle involve small shifts in the position of two of the helices (F and G) relative to the others. Thus, the small sliding motions in bacteriorhodopsin, as well as that in the aspartate receptor, appear to be consistent with a shear mechanism.

Particular values describing motion Creation Date = 19970822 Experimental Methods = e (Electron Diffraction) Modification Date = 1999-08-23 13:06:58.000

References R Henderson, J M Baldwin, T A Ceska, F Zemlin, E Beckmann and K H Downing (1990). Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J Mol Biol. 213: 899-929. [Medline info for 90294303] S Subramaniam, M Gerstein, D Oesterhelt and R H Henderson (1993). Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. EMBO J. 12: 1-8. [Medline info for 93154310] S Subramaniam, M Gerstein, D Oesterhelt and R H Henderson (1993). Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. EMBO J. 12: 1-8. [Medline info for 10074413]

GO terms associated with structures Molecular function ion channel activity Cellular component membrane Biological process ion transport

Morphs

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Best representative Morph Morph name Structure #1 Structure #2 Residues [ ] [ ]

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu