7r8c
From Proteopedia
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==The structure of human ABCG1== | ==The structure of human ABCG1== | ||
| - | <StructureSection load='7r8c' size='340' side='right'caption='[[7r8c]]' scene=''> | + | <StructureSection load='7r8c' size='340' side='right'caption='[[7r8c]], [[Resolution|resolution]] 3.70Å' 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=7R8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7R8C FirstGlance]. <br> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7R8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7R8C FirstGlance]. <br> | ||
| - | </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=7r8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7r8c OCA], [https://pdbe.org/7r8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7r8c RCSB], [https://www.ebi.ac.uk/pdbsum/7r8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7r8c ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7Å</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=7r8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7r8c OCA], [https://pdbe.org/7r8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7r8c RCSB], [https://www.ebi.ac.uk/pdbsum/7r8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7r8c ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The ABCG1 homodimer (G1) and ABCG5-ABCG8 heterodimer (G5G8), two members of the adenosine triphosphate (ATP)-binding cassette (ABC) transporter G family, are required for maintenance of cellular cholesterol levels. G5G8 mediates secretion of neutral sterols into bile and the gut lumen, whereas G1 transports cholesterol from macrophages to high-density lipoproteins (HDLs). The mechanisms used by G5G8 and G1 to recognize and export sterols remain unclear. Here, we report cryoelectron microscopy (cryo-EM) structures of human G5G8 in sterol-bound and human G1 in cholesterol- and ATP-bound states. Both transporters have a sterol-binding site that is accessible from the cytosolic leaflet. A second site is present midway through the transmembrane domains of G5G8. The Walker A motif of G8 adopts a unique conformation that accounts for the marked asymmetry in ATPase activities between the two nucleotide-binding sites of G5G8. These structures, along with functional validation studies, provide a mechanistic framework for understanding cholesterol efflux via ABC transporters. | ||
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| + | Molecular basis of cholesterol efflux via ABCG subfamily transporters.,Sun Y, Wang J, Long T, Qi X, Donnelly L, Elghobashi-Meinhardt N, Esparza L, Cohen JC, Xie XS, Hobbs HH, Li X Proc Natl Acad Sci U S A. 2021 Aug 24;118(34). pii: 2110483118. doi:, 10.1073/pnas.2110483118. PMID:34404721<ref>PMID:34404721</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7r8c" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
The structure of human ABCG1
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Categories: Large Structures | Li X | Long T | Sun Y
