Refinement of the Geometry of the Retinal Binding Pocket in Dark-Adapted Bacteriorhodopsin by Heteronuclear Solid-State NMR Distance Measurements

Refinement of the Geometry of the Retinal Binding Pocket in Dark-Adapted Bacteriorhodopsin by Heteronuclear Solid-State NMR Distance Measurements

The bacterial proton pump bacteriorhodopsin (BR) is a 26.5 kDa seven-transmembrane helical protein. Several structural models have been published at ≥1.55 Å resolution. The initial cis−trans isomerization of the retinal moiety involves structural changes within

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Veröffentlicht in:Biochemistry (Easton) 2000-08, Vol.39 (33), p.10066-10071
Hauptverfasser: Helmle, Michael, Patzelt, Heiko, Ockenfels, Andreas, Gärtner, Wolfgang, Oesterhelt, Dieter, Bechinger, Burkhard
Format: Artikel
Sprache:eng
Schlagworte:
Bacteriorhodopsins - chemistry
Bacteriorhodopsins - metabolism
Binding Sites
Darkness
Halobacterium
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular
Proton Pumps - chemistry
Proton Pumps - metabolism
retinal binding pocket
Retinaldehyde - chemistry
Retinaldehyde - metabolism
Subcellular Fractions - chemistry
Subcellular Fractions - metabolism
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Zusammenfassung:The bacterial proton pump bacteriorhodopsin (BR) is a 26.5 kDa seven-transmembrane helical protein. Several structural models have been published at ≥1.55 Å resolution. The initial cis−trans isomerization of the retinal moiety involves structural changes within
ISSN:0006-2960
1520-4995
DOI:10.1021/bi0006666