Structure of the Glycosyltransferase Ktr4p from Saccharomyces cerevisiae.

In the yeast Saccharomyces cerevisiae, members of the Kre2/Mnt1 protein family have been shown to be α-1,2-mannosyltransferases or α-1,2-mannosylphosphate transferases, utilising an Mn2+-coordinated GDP-mannose as the sugar donor and a variety of mannose derivatives as acceptors. Enzymes in this family are localised to the Golgi apparatus, and have been shown to be involved in both N- and O-linked glycosylation of newly-synthesised proteins, including cell wall glycoproteins. Our knowledge of the nine proteins in this family is however very incomplete at present.

Purification, crystallization and preliminary X-ray crystallographic analysis of the lumenal domain of the ER-vesicle protein Erv41p from Saccharomyces cerevisiae.

The membrane protein Erv41p is a major component of COPII-coated vesicles and is thought to play a role in the early secretory pathway in eukaryotic cells. In this study, the full lumenal domain of Erv41p from Saccharomyces cerevisiae (ScErv41p_LD) was recombinantly expressed in Sf9 insect cells and purified by nickel-affinity, ion-exchange and size-exclusion chromatography. ScErv41p_LD crystals were obtained using the sitting-drop vapour-diffusion method and native X-ray diffraction data were collected to 2.

The crystal structure of the lumenal domain of Erv41p, a protein involved in transport between the endoplasmic reticulum and Golgi apparatus.

Erv41p is a conserved integral membrane protein that is known to play a role in transport between the endoplasmic reticulum and Golgi apparatus, part of the early secretory pathway of eukaryotes. However, the exact function of the protein is not known, and it shares very low sequence identity with proteins of known structure or function. Here we present the structure of the full lumenal domain of Erv41p from Saccharomyces cerevisiae, determined by X-ray crystallography to a resolution of 2.