title: Unusual armadillo fold in the human general vesicular transport factor p115.
abstract: The golgin family gives identity and structure to the Golgi apparatus and is part of a complex protein network at the Golgi membrane. The golgin p115 is targeted by the GTPase Rab1a, contains a large globular head region and a long region of coiled-coil which forms an extended rod-like structure. p115 serves as vesicle tethering factor and plays an important role at different steps of vesicular transport. Here we present the 2.2 A-resolution X-ray structure of the globular head region of p115. The structure exhibits an armadillo fold that is decorated by elongated loops and carries a C-terminal non-canonical repeat. This terminal repeat folds into the armadillo superhelical groove and allows homodimeric association with important implications for p115 mediated multiple protein interactions and tethering.
authors.affiliation: Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany.
authors.forename: Harald
authors.initials: H
authors.lastname: Striegl
authors.forename: Yvette
authors.initials: Y
authors.lastname: Roske
authors.forename: Daniel
authors.initials: D
authors.lastname: Kümmel
authors.forename: Udo
authors.initials: U
authors.lastname: Heinemann
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D000077614:Golgi Matrix Proteins; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017386:Sequence Homology, Amino Acid; D033921:Vesicular Transport Proteins / Q000737:chemistry* / Q000235:genetics
chemical_list: D000077614:Golgi Matrix Proteins; D033921:Vesicular Transport Proteins; C091580:vesicular transport factor p115