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. 2014 Dec 5;9(12):e112873. doi: 10.1371/journal.pone.0112873

Figure 7. Structure of the HmBRI trimer and its D-E loop.

Figure 7

(A) Comparison of the HmBRI trimer structure (green) with that of HsBR [23] (yellow). HmBRI trimer aligns well in the extracellular region, but the protomers are slightly rotated at the cytoplasmic side. (B) Magnification of the D-E loop. Unlike in other trimerizing retinylidene proteins, in HmBRI the loop is extended and makes contact to the adjacent protomer. (C) Wall-eyed stereogram of the HmBRI D-E loop. The adjacent protomer is shown in orange and its residues are marked by a prime. Three structural water molecules are observed that stabilize the loop structure.