3wme: Difference between revisions

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<StructureSection load='3wme' size='340' side='right'caption='[[3wme]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
<StructureSection load='3wme' size='340' side='right'caption='[[3wme]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3wme]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cyam1 Cyam1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WME FirstGlance]. <br>
<table><tr><td colspan='2'>[[3wme]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cyanidioschyzon_merolae_strain_10D Cyanidioschyzon merolae strain 10D]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WME FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</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]] 2.751&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wmf|3wmf]], [[3wmg|3wmg]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CMD148C, CYME_CMD148C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=280699 CYAM1])</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=3wme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wme OCA], [https://pdbe.org/3wme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wme RCSB], [https://www.ebi.ac.uk/pdbsum/3wme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wme 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=3wme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wme OCA], [https://pdbe.org/3wme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wme RCSB], [https://www.ebi.ac.uk/pdbsum/3wme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wme ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/M1VAN7_CYAM1 M1VAN7_CYAM1]
P-glycoprotein is an ATP-binding cassette multidrug transporter that actively transports chemically diverse substrates across the lipid bilayer. The precise molecular mechanism underlying transport is not fully understood. Here, we present crystal structures of a eukaryotic P-glycoprotein homolog, CmABCB1 from Cyanidioschyzon merolae, in two forms: unbound at 2.6-A resolution and bound to a unique allosteric inhibitor at 2.4-A resolution. The inhibitor clamps the transmembrane helices from the outside, fixing the CmABCB1 structure in an inward-open conformation similar to the unbound structure, confirming that an outward-opening motion is required for ATP hydrolysis cycle. These structures, along with site-directed mutagenesis and transporter activity measurements, reveal the detailed architecture of the transporter, including a gate that opens to extracellular side and two gates that open to intramembranous region and the cytosolic side. We propose that the motion of the nucleotide-binding domain drives those gating apparatuses via two short intracellular helices, IH1 and IH2, and two transmembrane helices, TM2 and TM5.
 
Structural basis for gating mechanisms of a eukaryotic P-glycoprotein homolog.,Kodan A, Yamaguchi T, Nakatsu T, Sakiyama K, Hipolito CJ, Fujioka A, Hirokane R, Ikeguchi K, Watanabe B, Hiratake J, Kimura Y, Suga H, Ueda K, Kato H Proc Natl Acad Sci U S A. 2014 Mar 3. PMID:24591620<ref>PMID:24591620</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wme" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cyam1]]
[[Category: Cyanidioschyzon merolae strain 10D]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kato, H]]
[[Category: Kato H]]
[[Category: Kodan, A]]
[[Category: Kodan A]]
[[Category: Nakatsu, T]]
[[Category: Nakatsu T]]
[[Category: Yamaguchi, T]]
[[Category: Yamaguchi T]]
[[Category: Multi drug transporter]]
[[Category: Rec fold]]
[[Category: Transport protein]]

Latest revision as of 08:45, 20 March 2024

Crystal structure of an inward-facing eukaryotic ABC multidrug transporter

3wme, resolution 2.75Å

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