3wmf

<StructureSection load='3wmf' size='340' side='right'caption='[[3wmf]], [[Resolution|resolution]] 2.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[3wmf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WMF 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>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wmf OCA], [https://pdbe.org/3wmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wmf RCSB], [https://www.ebi.ac.uk/pdbsum/3wmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wmf ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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>

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<div class="pdbe-citations 3wmf" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Kato, H]]

[[Category: Kodan, A]]

[[Category: Nakatsu, T]]

[[Category: Yamaguchi, T]]

[[Category: Transport protein]]