title: Structure of a bacterial cytoplasmic cyclophilin A in complex with a tetrapeptide.
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.
authors.affiliation: Physics Laboratory, Department of Science, Agricultural University of Athens, Iera Odos 75, 11855 Athens, Greece.
authors.forename: Elias
authors.initials: E
authors.lastname: Christoforides
authors.forename: Maria
authors.initials: M
authors.lastname: Dimou
authors.forename: Panagiotis
authors.initials: P
authors.lastname: Katinakis
authors.forename: Kostas
authors.initials: K
authors.lastname: Bethanis
authors.forename: Michael
authors.initials: M
authors.lastname: Karpusas
mesh_terms: D000595:Amino Acid Sequence; D016948:Azotobacter vinelandii / Q000201:enzymology*; D021984:Cyclophilin A / Q000737:chemistry*; D003593:Cytoplasm / Q000737:chemistry; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D054730:Protein Interaction Domains and Motifs; D016415:Sequence Alignment
chemical_list: D010455:Peptides; D021984:Cyclophilin A