6l48
From Proteopedia
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==Structure of the human sterol O-acyltransferase 1 in resting state== | ==Structure of the human sterol O-acyltransferase 1 in resting state== | ||
| - | <StructureSection load='6l48' size='340' side='right'caption='[[6l48]]' scene=''> | + | <StructureSection load='6l48' size='340' side='right'caption='[[6l48]], [[Resolution|resolution]] 3.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L48 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6L48 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6l48]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L48 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6L48 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6l48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l48 OCA], [http://pdbe.org/6l48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l48 RCSB], [http://www.ebi.ac.uk/pdbsum/6l48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l48 ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SOAT1, ACACT, ACACT1, ACAT, ACAT1, SOAT, STAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sterol_O-acyltransferase Sterol O-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.26 2.3.1.26] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6l48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l48 OCA], [http://pdbe.org/6l48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l48 RCSB], [http://www.ebi.ac.uk/pdbsum/6l48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l48 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SOAT1_HUMAN SOAT1_HUMAN]] Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sterol O-acyltransferase 1 (SOAT1) is an endoplasmic reticulum (ER) resident, multi-transmembrane enzyme that belongs to the membrane-bound O-acyltransferase (MBOAT) family. It catalyzes the esterification of cholesterol to generate cholesteryl esters for cholesterol storage. SOAT1 is a target to treat several human diseases. However, its structure and mechanism remain elusive since its discovery. Here, we report the structure of human SOAT1 (hSOAT1) determined by cryo-EM. hSOAT1 is a tetramer consisted of a dimer of dimer. The structure of hSOAT1 dimer at 3.5 A resolution reveals that a small molecule inhibitor CI-976 binds inside the catalytic chamber and blocks the accessibility of the active site residues H460, N421 and W420. Our results pave the way for future mechanistic study and rational drug design targeting hSOAT1 and other mammalian MBOAT family members. | ||
| + | |||
| + | Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor.,Guan C, Niu Y, Chen SC, Kang Y, Wu JX, Nishi K, Chang CCY, Chang TY, Luo T, Chen L Nat Commun. 2020 May 18;11(1):2478. doi: 10.1038/s41467-020-16288-4. PMID:32424158<ref>PMID:32424158</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6l48" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Chen L]] | + | [[Category: Sterol O-acyltransferase]] |
| - | [[Category: Guan C]] | + | [[Category: Chen, L]] |
| - | [[Category: Niu Y]] | + | [[Category: Guan, C]] |
| + | [[Category: Niu, Y]] | ||
| + | [[Category: Acat]] | ||
| + | [[Category: Mboat]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Soat]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 06:29, 7 October 2020
Structure of the human sterol O-acyltransferase 1 in resting state
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Categories: Human | Large Structures | Sterol O-acyltransferase | Chen, L | Guan, C | Niu, Y | Acat | Mboat | Membrane protein | Soat | Transferase
