Differences in the water channels in bacteriorhodopsin from the retinal to the outside surface

The two jmol windows are "sync"-ed.

Ground state Bacteriorhodopsin

Retinal, colored yellow

α-helices, colored magenta

Waters, colored black

Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin.
Sass HJ, Büldt G, Gessenich R, Hehn D, Neff D, Schlesinger R, Berendzen J, Ormos P.
Nature. 2000 Aug 10;406(6796):649-53.
(PubMed)

1cwq (PDB)

 Notice that there are more water molecules below the retinal and the Lys 216 in the protein on the right. This is the opened water channel that allows protons to be released to the outside.

M state Bacteriorhodopsin

Retinal, colored yellow

α-helices, colored magenta

Waters, colored black

Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin.
Sass HJ, Büldt G, Gessenich R, Hehn D, Neff D, Schlesinger R, Berendzen J, Ormos P.
Nature. 2000 Aug 10;406(6796):649-53. (PubMed)

1cwq (PDB)

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