Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin

Hans Jürgen Sass, Georg Büldt (), Ralf Gessenich, Dominic Hehn, Dirk Neff, Ramona Schlesinger, Joel Berendzen and Pal Ormos
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Hans Jürgen Sass: Institute of Structural Biology, Research Centre Jülich
Georg Büldt: Institute of Structural Biology, Research Centre Jülich
Ralf Gessenich: Institute of Structural Biology, Research Centre Jülich
Dominic Hehn: Institute of Structural Biology, Research Centre Jülich
Dirk Neff: Institute of Structural Biology, Research Centre Jülich
Ramona Schlesinger: Institute of Structural Biology, Research Centre Jülich
Joel Berendzen: Biophysics Group, Mail Stop D454, Los Alamos Laboratory
Pal Ormos: Institute of Biophysics, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, PO Box 521

Nature, 2000, vol. 406, issue 6796, 649-653

Abstract: Abstract The transport of protons across membranes is an important process in cellular bioenergetics. The light-driven proton pump bacteriorhodopsin is the best-characterized protein providing this function. Photon energy is absorbed by the chromophore retinal, covalently bound to Lys 216 via a protonated Schiff base. The light-induced all-trans to 13-cis isomerization of the retinal results in deprotonation of the Schiff base followed by alterations in protonatable groups within bacteriorhodopsin. The changed force field induces changes, even in the tertiary structure1,2,3, which are necessary for proton pumping. The recent report4 of a high-resolution X-ray crystal structure for the late M intermediate of a mutant bacteriorhopsin (with Asp 96→Asn) displays the structure of a proton pathway highly disturbed by the mutation. To observe an unperturbed proton pathway, we determined the structure of the late M intermediate of wild-type bacteriorhodopsin (2.25 Å resolution). The cytoplasmic side of our M2 structure shows a water net that allows proton transfer from the proton donor group Asp 96 towards the Schiff base. An enlarged cavity system above Asp 96 is observed, which facilitates the de- and reprotonation of this group by fluctuating water molecules in the last part of the cycle.

Date: 2000
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DOI: 10.1038/35020607

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