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TitleStructural Insight into Eukaryotic Sterol Transport through Niemann-Pick Type C Proteins.
Journal, issue, pagesCell, Vol. 179, Issue 2, Page 485-497.e18, Year 2019
Publish dateOct 3, 2019
AuthorsMikael B L Winkler / Rune T Kidmose / Maria Szomek / Katja Thaysen / Shaun Rawson / Stephen P Muench / Daniel Wüstner / Bjørn Panyella Pedersen /
PubMed AbstractNiemann-Pick type C (NPC) proteins are essential for sterol homeostasis, believed to drive sterol integration into the lysosomal membrane before redistribution to other cellular membranes. Here, ...Niemann-Pick type C (NPC) proteins are essential for sterol homeostasis, believed to drive sterol integration into the lysosomal membrane before redistribution to other cellular membranes. Here, using a combination of crystallography, cryo-electron microscopy, and biochemical and in vivo studies on the Saccharomyces cerevisiae NPC system (NCR1 and NPC2), we present a framework for sterol membrane integration. Sterols are transferred between hydrophobic pockets of vacuolar NPC2 and membrane-protein NCR1. NCR1 has its N-terminal domain (NTD) positioned to deliver a sterol to a tunnel connecting NTD to the luminal membrane leaflet 50 Å away. A sterol is caught inside this tunnel during transport, and a proton-relay network of charged residues in the transmembrane region is linked to this tunnel supporting a proton-driven transport mechanism. We propose a model for sterol integration that clarifies the role of NPC proteins in this essential eukaryotic pathway and that rationalizes mutations in patients with Niemann-Pick disease type C.
External linksCell / PubMed:31543266
MethodsEM (single particle) / X-ray diffraction
Resolution2.8 - 7.2 Å
Structure data

EMDB-4771:
S. cerevisiae Niemann-Pick type C Related Protein 1 (NCR1)
Method: EM (single particle) / Resolution: 7.2 Å

PDB-6r4l:
Crystal structure of S. cerevisia Niemann-Pick type C protein NCR1
Method: X-RAY DIFFRACTION / Resolution: 3.5 Å

PDB-6r4m:
Crystal structure of S. cerevisia Niemann-Pick type C protein NPC2
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-6r4n:
Crystal structure of S. cerevisia Niemann-Pick type C protein NPC2 with ergosterol bound
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

ChemComp-ERG:
ERGOSTEROL

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-SO4:
SULFATE ION

Source
  • Saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsLIPID TRANSPORT / Vacuole / Ergosterol / membrane protein

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