Sandbox Reserved 819: Difference between revisions
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==Introduction== | |||
Archaerhodopsin-2 (aR2) is a light-driven proton pump. The resulting proton gradient is subsequently converted into chemical energy. | |||
It is composed of 259 amino acids. 88% of this amino acid sequence is identical to the sequence of the archaerhodopsin. Moreover, there is 56% identity between this sequence and the sequence of the bacteriorhodopsin. <ref>PMID: 1654776</ref> | |||
==The trimeric structure of Archaerhodopsin-2== | ==The trimeric structure of Archaerhodopsin-2== | ||
Archaerhodopsin-2 is a retinal protein–carotenoid complex found in the claret membrane of Halorubrum sp. aus-2 and it represents a real adaptation to life at high salt concentrations. In these membranes, three Archaerhodopsin-2 chains form a trimeric structure [http://www.pdb.org/pdb/explore/jmol.do?structureId=2Z55&view=symmetry&bionumber=1], capturing light energy and using it to move protons across the membrane out of the cell. It exists four different chains with different structures: A,B,D,E (they are not represented here). | Archaerhodopsin-2 is a retinal protein–carotenoid complex found in the claret membrane of Halorubrum sp. aus-2 and it represents a real adaptation to life at high salt concentrations. In these membranes, three Archaerhodopsin-2 chains form a trimeric structure [http://www.pdb.org/pdb/explore/jmol.do?structureId=2Z55&view=symmetry&bionumber=1], capturing light energy and using it to move protons across the membrane out of the cell. It exists four different chains with different structures: A,B,D,E (they are not represented here). | ||
