View source for 7dqv


==Crystal structure of a CmABCB1 mutant==
<StructureSection load='7dqv' size='340' side='right'caption='[[7dqv]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7dqv]] 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=7DQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DQV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=7dqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dqv OCA], [https://pdbe.org/7dqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dqv RCSB], [https://www.ebi.ac.uk/pdbsum/7dqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dqv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/M1VAN7_CYAM1 M1VAN7_CYAM1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CmABCB1 is a homologue of human P-glycoprotein, which extrudes various substrates by iterative cycles of conformational changes between the inward- and outward-facing states. Comparison of the inward- and outward-facing structures of CmABCB1 suggested that pivotal joints in the transmembrane domain regulate the tilt of transmembrane helices. Transmembrane helix 1 (TM1) forms a tight helix-helix contact with TM3 at the TM1-3 joint. Mutation of Gly132 to valine at the TM1-3 joint, G132V, caused a 10-fold increase in ATPase activity, but the mechanism underlying this change remains unclear. Here, we report a crystal structure of the outward-facing state of the CmABCB1 G132V mutant at a 2.15 A resolution. We observed structural displacements between the outward-facing states of G132V and the previous one at the region around the TM1-3 joint, and a significant expansion at the extracellular gate. We hypothesize that steric hindrance caused by the Val substitution shifted the conformational equilibrium toward the outward-facing state, favoring the dimeric state of the nucleotide-binding domains and thereby increasing the ATPase activity of the G132V mutant.

The crystal structure of the CmABCB1 G132V mutant, which favors the outward-facing state, reveals the mechanism of the pivotal joint between TM1 and TM3.,Matsuoka K, Nakatsu T, Kato H Protein Sci. 2021 Mar 8. doi: 10.1002/pro.4058. PMID:33683740<ref>PMID:33683740</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7dqv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cyanidioschyzon merolae strain 10D]]
[[Category: Large Structures]]
[[Category: Kato H]]
[[Category: Matsuoka K]]
[[Category: Nakatsu T]]