5OGE

Crystal structure of a nucleotide sugar transporter

Summary for 5OGE

• Entry DOI: 10.2210/pdb5oge/pdb
• Descriptor: GDP-mannose transporter 1, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate (2 entities in total)
• Functional Keywords: slc35, golgi transporter, membrane protein
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Cellular location: Golgi apparatus membrane; Multi-pass membrane protein: P40107
• Total number of polymer chains: 8
• Total formula weight: 300634.51

Authors

Newstead, S.,Parker, J.L. (deposition date: 2017-07-12, release date: 2017-11-22, Last modification date: 2024-05-08)

Primary citation

Parker, J.L.,Newstead, S.
Structural basis of nucleotide sugar transport across the Golgi membrane.
Nature, 551:521-524, 2017

PubMed Abstract: Glycosylation is a fundamental cellular process that, in eukaryotes, occurs in the lumen of both the Golgi apparatus and the endoplasmic reticulum. Nucleotide sugar transporters (NSTs) are an essential component of the glycosylation pathway, providing the diverse range of substrates required for the glycosyltransferases. NSTs are linked to several developmental and immune disorders in humans, and in pathogenic microbes they have an important role in virulence. How NSTs recognize and transport activated monosaccharides, however, is currently unclear. Here we present the crystal structure of an NST, the GDP-mannose transporter Vrg4, in both the substrate-free and the bound states. A hitherto unobserved requirement of short-chain lipids in activating the transporter supports a model for regulation within the highly dynamic membranes of the Golgi apparatus. Our results provide a structural basis for understanding nucleotide sugar recognition, and provide insights into the transport and regulatory mechanism of this family of intracellular transporters.

PubMed: 29143814
DOI: 10.1038/nature24464

Experimental method

X-RAY DIFFRACTION (3.22 Å)