Sandbox Reserved 819: Difference between revisions

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=2Z55=

__TOC__

==Introduction==

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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 ~~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 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.

Sandbox Reserved 819: Difference between revisions

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 {{Sandbox_Reserved_ESBS}}
 <!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
 <StructureSection load='2z55' size='300' side='right' caption='2z55: cristal made of four Archaerhodopsin-2' scene=''>
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+__TOC__
 ==Introduction==
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 % 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 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 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.