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6r4l

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'''Unreleased structure'''
 
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The entry 6r4l is ON HOLD
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==Crystal structure of S. cerevisia Niemann-Pick type C protein NCR1==
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<StructureSection load='6r4l' size='340' side='right'caption='[[6r4l]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6r4l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R4L FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NCR1, YPL006W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6r4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r4l OCA], [http://pdbe.org/6r4l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r4l RCSB], [http://www.ebi.ac.uk/pdbsum/6r4l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r4l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6r4l" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Baker's yeast]]
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[[Category: Large Structures]]
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[[Category: Kidmose, R T]]
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[[Category: Pedersen, B P]]
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[[Category: Winkler, M B.L]]
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[[Category: Ergosterol]]
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[[Category: Lipid transport]]
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[[Category: Membrane protein]]
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[[Category: Vacuole]]

Revision as of 07:38, 16 October 2019

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

PDB ID 6r4l

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