Sandbox Reserved 819: Difference between revisions
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56% of the Archaeorhodopsin-2 sequence is identical to the [[Bacteriorhodopsin]] sequence.<ref name="seq">PMID: 1654776</ref> | 56% of the Archaeorhodopsin-2 sequence is identical to the [[Bacteriorhodopsin]] sequence.<ref name="seq">PMID: 1654776</ref> | ||
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 | 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 polar 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. The interaction between the monomers of the Bacteriorhodopsin is also mediated by lipids: diphytanyl diether phospholipids instead of Bacterioruberin. | 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. | ||
