4quv
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4quv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylotuvimicrobium_alcaliphilum_20Z Methylotuvimicrobium alcaliphilum 20Z]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QUV FirstGlance]. <br> | <table><tr><td colspan='2'>[[4quv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylotuvimicrobium_alcaliphilum_20Z Methylotuvimicrobium alcaliphilum 20Z]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QUV FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.743Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</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=4quv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4quv OCA], [https://pdbe.org/4quv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4quv RCSB], [https://www.ebi.ac.uk/pdbsum/4quv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4quv ProSAT]</span></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=4quv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4quv OCA], [https://pdbe.org/4quv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4quv RCSB], [https://www.ebi.ac.uk/pdbsum/4quv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4quv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ERG_META2 ERG_META2] Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. Complements the deletion of the Delta(14)-sterol reductase gene ERG24 in yeast.<ref>PMID:25307054</ref> | [https://www.uniprot.org/uniprot/ERG_META2 ERG_META2] Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. Complements the deletion of the Delta(14)-sterol reductase gene ERG24 in yeast.<ref>PMID:25307054</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Sterols are essential biological molecules in the majority of life forms. Sterol reductases including Delta14-sterol reductase (C14SR, also known as TM7SF2), 7-dehydrocholesterol reductase (DHCR7) and 24-dehydrocholesterol reductase (DHCR24) reduce specific carbon-carbon double bonds of the sterol moiety using a reducing cofactor during sterol biosynthesis. Lamin B receptor (LBR), an integral inner nuclear membrane protein, also contains a functional C14SR domain. Here we report the crystal structure of a Delta14-sterol reductase (MaSR1) from the methanotrophic bacterium Methylomicrobium alcaliphilum 20Z (a homologue of human C14SR, LBR and DHCR7) with the cofactor NADPH. The enzyme contains ten transmembrane segments (TM1-10). Its catalytic domain comprises the carboxy-terminal half (containing TM6-10) and envelops two interconnected pockets, one of which faces the cytoplasm and houses NADPH, while the other one is accessible from the lipid bilayer. Comparison with a soluble steroid 5beta-reductase structure suggests that the reducing end of NADPH meets the sterol substrate at the juncture of the two pockets. A sterol reductase activity assay proves that MaSR1 can reduce the double bond of a cholesterol biosynthetic intermediate, demonstrating functional conservation to human C14SR. Therefore, our structure as a prototype of integral membrane sterol reductases provides molecular insight into mutations in DHCR7 and LBR for inborn human diseases. | ||
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| - | Structure of an integral membrane sterol reductase from Methylomicrobium alcaliphilum.,Li X, Roberti R, Blobel G Nature. 2014 Oct 12. doi: 10.1038/nature13797. PMID:25307054<ref>PMID:25307054</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4quv" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Structure of an integral membrane delta(14)-sterol reductase
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