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INDHUMATHI. J
14MG05
Milestones in BR Structural
Determination
In order to assess the structure and
mechanism of BR, or any membrane
protein, we really need to understand
its tertiary structure by X-ray
crystallography
BUT, membrane proteins dont
crystallize easily
Michel
First to
crystallize BR
in 1980
Contribution
to
determination
of structure of
a
photosynthetic
reaction
center earned
him a Nobel
Findings
Could get protein crystallization
Crystals were too small and
disordered to determine tertiary
structure
1990
Henderson et al. use cryocrystallography to study BR
Crystallization occurred
First instances of structural
determination
However, some areas of the protein
could not be resolved
BACTERIORHODOPSIN
Biological
macromolecule
Integral
membrane protein
Simple cell
membrane
receptor
G-protein coupled
seven helix
receptors
Structural Info
7 TM helices
Forms a homotrimer
Homotrimers aggregate to form the purple
membrane
Each bacteriorhodopsin contains one
molecule of a linear pigment called retinal
Stability of trimer by:
G113, I117, L48
Most stability comes from surrounding lipids
FUNCTION
STRUCTURE
RETINAL
RETINAL
The light interacting group in BR is a
retinylidene residue attached via a Schiff base
linkage to the protein moiety.
one end is attached to the nitrogen atom of a
lysine residue in helix G and the other end is
wedged deep in the protein.
Retinal changes its structure in response to
visible light.
The polypeptide harnesses the light energy
trapped by the retinal and uses it to push a
single proton through the seven-helix bundle,
from the cell interior to the outside.
MECHANISM
ISOMERISATION OF RETINAL
Thank you