Wilmann, Pascal G., Battad, Jion, Beddoe, Travis, Olsen, Seth, Smith, Sean C., Dove, Sophie, Devenish, Rodney J., Rossjohn, Jamie, and Prescott, Mark (2006) The 2.0 Å crystal structure of a pocilloporin at pH 3.5: the structural basis for the linkage between color transition and halide binding. Photochemistry and Photobiology, 82 (2). pp. 359-366.

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Abstract

The pocilloporin Rtms5 and an engineered variant Rtms5 H146S undergo distinct color transitions (from blue to red to yellow to colorless) in a pH-dependent manner. pKa values of 4.1 and 3.2 were determined for the blue (absorption Λmax, 590 nm) to yellow (absorption Λmax, ~453 nm) transitions of Rtms5 and Rtms5 H146. The pKa for the blue-yellow transition of Rtms5 H146S increased by 1.4 U in the presence of 0.1 M KI, whereas the pKa for the same transition of Rtms5 was relatively insensitive to added halides. To understand the structural basis for these observations, we have determined to 2.0 Å resolution the crystal structure of a yellow form of Rtms5 H146S at pH 3.5 in the presence of iodide. Iodide was found occupying a pocket in the structure with a pH of 3.5, forming van der Waals contacts with the tyrosyl moiety of the chromophore. Elsewhere, it was determined that this pocket is occupied by a water molecule in the Rtms5 H146S structure (pH 8.0) and by the side chain of histidine 146 in the wild-type Rtms5 structure. Collectively, our data provide an explanation for the observed linkage between color transitions for Rtms5 H146S and binding to halides.

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