6QSK

Crystal structure of a nucleotide sugar transporter with bound nucleotide monophosphate.

Summary for 6QSK

• Entry DOI: 10.2210/pdb6qsk/pdb
• Related: 5OGE 5OGK
• Descriptor: GDP-mannose transporter 1, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, GUANOSINE-5'-MONOPHOSPHATE, ... (5 entities in total)
• Functional Keywords: golgi transporter; slc35; gdp-mannose transport; glycosylation, membrane protein
• Biological source: Saccharomyces cerevisiae S288C
• Total number of polymer chains: 8
• Total formula weight: 298181.77

Authors

Newstead, S.,Parker, J.L. (deposition date: 2019-02-21, release date: 2019-10-02, Last modification date: 2024-01-24)

Primary citation

Parker, J.L.,Corey, R.A.,Stansfeld, P.J.,Newstead, S.
Structural basis for substrate specificity and regulation of nucleotide sugar transporters in the lipid bilayer.
Nat Commun, 10:4657-4657, 2019

PubMed Abstract: Nucleotide sugars are the activated form of monosaccharides used by glycosyltransferases during glycosylation. In eukaryotes the SLC35 family of solute carriers are responsible for their selective uptake into the Endoplasmic Reticulum or Golgi apparatus. The structure of the yeast GDP-mannose transporter, Vrg4, revealed a requirement for short chain lipids and a marked difference in transport rate between the nucleotide sugar and nucleoside monophosphate, suggesting a complex network of regulatory elements control transport into these organelles. Here we report the crystal structure of the GMP bound complex of Vrg4, revealing the molecular basis for GMP recognition and transport. Molecular dynamics, combined with biochemical analysis, reveal a lipid mediated dimer interface and mechanism for coordinating structural rearrangements during transport. Together these results provide further insight into how SLC35 family transporters function within the secretory pathway and sheds light onto the role that membrane lipids play in regulating transport across the membrane.

PubMed: 31604945
DOI: 10.1038/s41467-019-12673-w

Experimental method

X-RAY DIFFRACTION (3.394 Å)