6bhu
From Proteopedia
(Difference between revisions)
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<StructureSection load='6bhu' size='340' side='right' caption='[[6bhu]], [[Resolution|resolution]] 3.14Å' scene=''> | <StructureSection load='6bhu' size='340' side='right' caption='[[6bhu]], [[Resolution|resolution]] 3.14Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6bhu]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BHU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BHU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6bhu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BHU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BHU FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uj9|5uj9]], [[5uja|5uja]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uj9|5uj9]], [[5uja|5uja]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABCC1, MRP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr> | ||
<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=6bhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bhu OCA], [http://pdbe.org/6bhu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bhu RCSB], [http://www.ebi.ac.uk/pdbsum/6bhu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bhu ProSAT]</span></td></tr> | <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=6bhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bhu OCA], [http://pdbe.org/6bhu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bhu RCSB], [http://www.ebi.ac.uk/pdbsum/6bhu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bhu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The multidrug resistance protein MRP1 is an ATP-driven pump that confers resistance to chemotherapy. Previously, we have shown that intracellular substrates are recruited to a bipartite binding site when the transporter rests in an inward-facing conformation. A key question remains: how are high-affinity substrates transferred across the membrane and released outside the cell? Using electron cryomicroscopy, we show here that ATP binding opens the transport pathway to the extracellular space and reconfigures the substrate-binding site such that it relinquishes its affinity for substrate. Thus, substrate is released prior to ATP hydrolysis. With this result, we now have a complete description of the conformational cycle that enables substrate transfer in a eukaryotic ABC exporter. | ||
| + | |||
| + | ATP Binding Enables Substrate Release from Multidrug Resistance Protein 1.,Johnson ZL, Chen J Cell. 2018 Jan 11;172(1-2):81-89.e10. doi: 10.1016/j.cell.2017.12.005. Epub 2017 , Dec 28. PMID:29290467<ref>PMID:29290467</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6bhu" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bovin]] | ||
[[Category: Chen, J]] | [[Category: Chen, J]] | ||
[[Category: Johnson, Z L]] | [[Category: Johnson, Z L]] | ||
Revision as of 08:25, 17 January 2018
Cryo-EM structure of ATP-bound, outward-facing bovine multidrug resistance protein 1 (MRP1)
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