 |
PDBsum entry 5oge
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Membrane protein
|
PDB id
|
|
|
|
5oge
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Membrane protein
|
|
|
Title:
|
|
Crystal structure of a nucleotide sugar transporter
|
|
Structure:
|
|
Gdp-mannose transporter 1. Chain: a, b, c, d, e, f, g, h. Synonym: gmt 1,low dye-binding protein 3,morphogenesis checkpoint- dependent protein 3,vanadate resistance glycosylation protein 4. Engineered: yes
|
|
Source:
|
|
Saccharomyces cerevisiae (strain atcc 204508 / s288c). Baker's yeast. Organism_taxid: 559292. Gene: vrg4, gog5, ldb3, mcd3, van2, vig4, ygl225w. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4930.
|
|
Resolution:
|
|
|
3.22Å
|
R-factor:
|
0.281
|
R-free:
|
0.306
|
|
|
Authors:
|
|
S.Newstead,J.L.Parker
|
|
Key ref:
|
|
J.L.Parker
and
S.Newstead
(2017).
Structural basis of nucleotide sugar transport across the Golgi membrane.
Nature,
551,
521-524.
PubMed id:
|
|
|
Date:
|
|
|
12-Jul-17
|
Release date:
|
22-Nov-17
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P40107
(GMT1_YEAST) -
GDP-mannose transporter 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
|
|
|
|
Seq:
Struc:
|
|
|
|
337 a.a.
299 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
Nature
551:521-524
(2017)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Structural basis of nucleotide sugar transport across the Golgi membrane.
|
|
J.L.Parker,
S.Newstead.
|
|
|
|
|
| |
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.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
