Structure of a bacterial cytoplasmic cyclophilin A in complex with a tetrapeptide
Elias Christoforides1, Maria Dimou, Panagiotis Katinakis
1Physics Laboratory, Department of Science, Agricultural University of Athens, Iera Odos 75, 11855 Athens, Greece.
Abstract:
Cyclophilins constitute a class of peptidyl-prolyl isomerases which participate in processes related to protein folding, signalling and chaperoning. The crystal structure of the cytoplasmic cyclophilin A (CyPA) from the bacterium Azotobacter vinelandii complexed with a synthetic tetrapeptide was determined by molecular replacement at 2 resolution. The proline in the tetrapeptide is observed to adopt the cis-isomer conformation. Comparisons of this structure with other CyPA structures provide insights into the conformational variability, effects of peptide binding and structure-function relationships of this enzyme.
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