Solution NMR Structure of Proteorhodopsin

and we show herein the de novo structure ofthegreenvariantofproteorhodopsinsolvedbysolutionNMRspectroscopy.The structure of PR (Figure 1) was solved in the short-chain lipid diC7PC (diheptanoyl-phosphocholine) combininglong-range NOEs with restraints derived from paramagneticrelaxation enhancement (PRE) and residual dipolar cou-plings (RDCs). The seven transmembrane helices are con-nected by short loops. Instead of the anti-parallel b-sheet thatis observed between helices B and C in other microbialrhodopsins, torsion angles derived from the protein backbonedihedral angle prediction program TALOS+ suggest that PRresidues G87–P90 form a short b-turn. The loop betweenhelices D and E is longer than predicted by the secondarystructure prediction program TMHMM.