The structure and mechanism of the family of retinal proteins from halophilic archaea.
Retinal proteins from halophilic archaea provide a unique opportunity to analyze vectorial ion translocation. Studies on its structure, conformational changes, proton conduction and electrogenic steps have helped to elucidate the catalytic cycle of bacteriorhodopsin in increasing detail. Experimental modulation of the vectoriality and ion specificity by altering the substrate availability, point mutations and light conditions for the different retinal proteins allows the proposal of a general model of ion transport for this protein family.
Oesterhelt
D
D
Max-Planck-Institut für Biochemie, Martinsried, Germany. oesterhe@biochem.mpg.de
D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism*; D001436:Bacteriorhodopsins / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D002338:Carotenoids; D025602:Halorhodopsins; D008958:Models, Molecular; D011487:Protein Conformation; D012172:Retinaldehyde / Q000737:chemistry* / Q000378:metabolism; D025603:Sensory Rhodopsins
D019843:Archaeal Proteins; D025602:Halorhodopsins; C061497:SRI protein, Halobacterium; D025603:Sensory Rhodopsins; C061508:sensory rhodopsin II protein, archaeal; D002338:Carotenoids; D001436:Bacteriorhodopsins; D012172:Retinaldehyde