6a6m

<StructureSection load='6a6m' size='340' side='right' caption='[[6a6m]], [[Resolution|resolution]] 1.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[6a6m]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A6M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A6M FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></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=6a6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a6m OCA], [http://pdbe.org/6a6m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a6m RCSB], [http://www.ebi.ac.uk/pdbsum/6a6m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a6m ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

P-glycoprotein extrudes a large variety of xenobiotics from the cell, thereby protecting tissues from their toxic effects. The machinery underlying unidirectional multidrug pumping remains unknown, largely due to the lack of high-resolution structural information regarding the alternate conformational states of the molecule. Here we report a pair of structures of homodimeric P-glycoprotein: an outward-facing conformational state with bound nucleotide and an inward-facing apo state, at resolutions of 1.9 A and 3.0 A, respectively. Features that can be clearly visualized at this high resolution include ATP binding with octahedral coordination of Mg(2+); an inner chamber that significantly changes in volume with the aid of tight connections among transmembrane helices (TM) 1, 3, and 6; a glutamate-arginine interaction that stabilizes the outward-facing conformation; and extensive interactions between TM1 and TM3, a property that distinguishes multidrug transporters from floppases. These structural elements are proposed to participate in the mechanism of the transporter.

 

Inward- and outward-facing X-ray crystal structures of homodimeric P-glycoprotein CmABCB1.,Kodan A, Yamaguchi T, Nakatsu T, Matsuoka K, Kimura Y, Ueda K, Kato H Nat Commun. 2019 Jan 8;10(1):88. doi: 10.1038/s41467-018-08007-x. PMID:30622258<ref>PMID:30622258</ref>

 

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<references/>

[[Category: Kato, H]]

[[Category: Kodan, A]]

[[Category: Nakatsu, T]]

[[Category: Transport protein]]

[[Category: Transport protein alpha-helical]]