6r4l

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of S. cerevisia Niemann-Pick type C protein NCR1

Structural highlights

6r4l is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.5Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NPC1_YEAST Involved in sphingolipid trafficking. May recycle sphingolipids between cellular membranous compartments.^[1] ^[2]

Publication Abstract from PubMed

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 A 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.

Structural Insight into Eukaryotic Sterol Transport through Niemann-Pick Type C Proteins.,Winkler MBL, Kidmose RT, Szomek M, Thaysen K, Rawson S, Muench SP, Wustner D, Pedersen BP Cell. 2019 Oct 3;179(2):485-497.e18. doi: 10.1016/j.cell.2019.08.038. Epub 2019, Sep 19. PMID:31543266^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Malathi K, Higaki K, Tinkelenberg AH, Balderes DA, Almanzar-Paramio D, Wilcox LJ, Erdeniz N, Redican F, Padamsee M, Liu Y, Khan S, Alcantara F, Carstea ED, Morris JA, Sturley SL. Mutagenesis of the putative sterol-sensing domain of yeast Niemann Pick C-related protein reveals a primordial role in subcellular sphingolipid distribution. J Cell Biol. 2004 Feb 16;164(4):547-56. PMID:14970192 doi:http://dx.doi.org/10.1083/jcb.200310046
↑ Berger AC, Hanson PK, Wylie Nichols J, Corbett AH. A yeast model system for functional analysis of the Niemann-Pick type C protein 1 homolog, Ncr1p. Traffic. 2005 Oct;6(10):907-17. PMID:16138904 doi:http://dx.doi.org/TRA327
↑ Winkler MBL, Kidmose RT, Szomek M, Thaysen K, Rawson S, Muench SP, Wustner D, Pedersen BP. Structural Insight into Eukaryotic Sterol Transport through Niemann-Pick Type C Proteins. Cell. 2019 Oct 3;179(2):485-497.e18. doi: 10.1016/j.cell.2019.08.038. Epub 2019, Sep 19. PMID:31543266 doi:http://dx.doi.org/10.1016/j.cell.2019.08.038

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6r4l"

Categories: Large Structures | Saccharomyces cerevisiae S288C | Kidmose RT | Pedersen BP | Winkler MBL

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6r4l is ON HOLD
+==Crystal structure of S. cerevisia Niemann-Pick type C protein NCR1==
+<StructureSection load='6r4l' size='340' side='right'caption='[[6r4l]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6r4l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6R4L FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=ERG:ERGOSTEROL'>ERG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6r4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r4l OCA], [https://pdbe.org/6r4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r4l RCSB], [https://www.ebi.ac.uk/pdbsum/6r4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r4l ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/NPC1_YEAST NPC1_YEAST] Involved in sphingolipid trafficking. May recycle sphingolipids between cellular membranous compartments.<ref>PMID:14970192</ref> <ref>PMID:16138904</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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 A 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.
-Authors:
+Structural Insight into Eukaryotic Sterol Transport through Niemann-Pick Type C Proteins.,Winkler MBL, Kidmose RT, Szomek M, Thaysen K, Rawson S, Muench SP, Wustner D, Pedersen BP Cell. 2019 Oct 3;179(2):485-497.e18. doi: 10.1016/j.cell.2019.08.038. Epub 2019, Sep 19. PMID:31543266<ref>PMID:31543266</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6r4l" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Saccharomyces cerevisiae S288C]]
+[[Category: Kidmose RT]]
+[[Category: Pedersen BP]]
+[[Category: Winkler MBL]]

6r4l

From Proteopedia

Current revision

Crystal structure of S. cerevisia Niemann-Pick type C protein NCR1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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