Crystal structure of a multi-domain immunophilin from Arabidopsis thaliana: a paradigm for regulation of plant ABC transporters.
FKBP42 is a membrane-anchored immunophilin playing a critical role in morphogenesis and development of higher plants. We present the X-ray structure of the cytoplasmic portion of FKBP42 comprising both the FKBP-like domain and the TPR domain at 2.85 A resolution. The data shed light on the probable binding modes of key interaction partners, including HSP90 and two classes of ABC transporters. The resulting models provide a structural background for further investigation of the unique biological properties of this protein.
Granzin
Joachim
J
Institute of Neurosciences and Biophysics, Molecular Biophysics, Research Centre Jülich, D-52425 Jülich, Germany.
Eckhoff
Andreas
A
Weiergräber
Oliver H
OH
D018528:ATP-Binding Cassette Transporters / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D003593:Cytoplasm; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism; D020104:Immunophilins / Q000737:chemistry*; D015394:Molecular Structure; D011485:Protein Binding; D011487:Protein Conformation; D022021:Tacrolimus Binding Proteins / Q000737:chemistry*
D018528:ATP-Binding Cassette Transporters; D029681:Arabidopsis Proteins; D018841:HSP90 Heat-Shock Proteins; C471286:TWD1 protein, Arabidopsis; D022021:Tacrolimus Binding Proteins; D020104:Immunophilins