%0 Journal Article
%T Low-resolution structure of the soluble domain GPAA1 (yGPAA170每247) of the glycosylphosphatidylinositol transamidase subunit GPAA1 from Saccharomyces cerevisiae
%A WuanˋGeok Saw
%A Birgit Eisenhaber
%A Frank Eisenhaber
%A Gerhard Gr邦ber
%J Bioscience Reports
%D 2013
%I Portland Press, Biochemical Society
%R 10.1042/bsr20120107
%X The GPI (glycosylphosphatidylinositol) transamidase complex catalyses the attachment of GPI anchors to eukaryotic proteins in the lumen of ER (endoplasmic reticulum). The Saccharomyces cerevisiae GPI transamidase complex consists of the subunits yPIG-K (Gpi8p), yPIG-S (Gpi17p), yPIG-T (Gpi16p), yPIG-U (CDC91/GAB1) and yGPAA1. We present the production of the two recombinant proteins yGPAA170每247 and yGPAA170每339 of the luminal domain of S. cerevisiae GPAA1, covering the amino acids 70每247 and 70每339 respectively. The secondary structural content of the stable and monodisperse yGPAA170每247 has been determined to be 28% 汐-helix and 27% 汕-sheet. SAXS (small-angle X-ray scattering) data showed that yGPAA170每247 has an Rg (radius of gyration) of 2.72㊣0.025 nm and Dmax (maximum dimension) of 9.14 nm. These data enabled the determination of the two domain low-resolution solution structure of yGPAA170每247. The large elliptical shape of yGPAA170每247 is connected via a short stalk to the smaller hook-like domain of 0.8 nm in length and 3.5 nm in width. The topological arrangement of yGPAA170每247 will be discussed together with the recently determined low-resolution structures of yPIG-K24每337 and yPIG-S38每467 from S. cerevisiae in the GPI transamidase complex.
%K glycosylphosphatidylinositol lipid anchor
%K glycosylphosphatidylinositol transamidase
%K GPAA1
%K PIG-K
%K PIG-S
%K post-translational modification
%U http://www.bioscirep.org/bsr/033/e033/bsr033e033.htm