Sandbox Reserved 819: Difference between revisions
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Most amino acids that play a role in the trimerization are not conserved between the two proteins. For instance, the counterparts of some hydrophobic residues of the Archaerhodopsin-2 (the one interacting with the polyene chain of the bacterioruberin) have a different volume. Another difference is the fact that the hydrophobic residues of the Archaerhodopsin-2 (responsible for the hydrogen bonds with the bacterioruberin) are replaced in the [[Bacteriorhodopsin]] by hydrophobic amino acids. | Most amino acids that play a role in the trimerization are not conserved between the two proteins. For instance, the counterparts of some hydrophobic residues of the Archaerhodopsin-2 (the one interacting with the polyene chain of the bacterioruberin) have a different volume. Another difference is the fact that the hydrophobic residues of the Archaerhodopsin-2 (responsible for the hydrogen bonds with the bacterioruberin) are replaced in the [[Bacteriorhodopsin]] by hydrophobic amino acids. | ||
However the global structures of Archaeorhodopsin-2 and [[Bacteriorhodopsin]] are really similar, especially at the level of the open space between the monomers. This similarity of structure forms the basis of several hypothesis concerning the mechanisms of the Archaeorhodopsin-2 <ref name="multiple">PMID:18082767</ref> | However the global structures of Archaeorhodopsin-2 and [[Bacteriorhodopsin]] are really similar, especially at the level of the open space between the monomers. The interaction between the monomers of the [[Bacteriorhodopsin]] is also mediated by lipids: diphytanyl diether phospholipids instead of Bacterioruberin. | ||
This similarity of structure forms the basis of several hypothesis concerning the mechanisms of the Archaeorhodopsin-2 <ref name="multiple">PMID:18082767</ref> | |||
