6csx: Difference between revisions

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<SX load='6csx' size='340' side='right' viewer='molstar' caption='[[6csx]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<SX load='6csx' size='340' side='right' viewer='molstar' caption='[[6csx]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6csx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CSX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6CSX FirstGlance]. <br>
<table><tr><td colspan='2'>[[6csx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CSX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D12:DODECANE'>D12</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acrB, acrE, b0462, JW0451 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D12:DODECANE'>D12</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6csx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6csx OCA], [http://pdbe.org/6csx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6csx RCSB], [http://www.ebi.ac.uk/pdbsum/6csx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6csx 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=6csx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6csx OCA], [https://pdbe.org/6csx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6csx RCSB], [https://www.ebi.ac.uk/pdbsum/6csx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6csx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ACRB_ECOLI ACRB_ECOLI]] AcrAB is a drug efflux protein with a broad substrate specificity.<ref>PMID:16915237</ref> <ref>PMID:16946072</ref> <ref>PMID:17194213</ref> 
[https://www.uniprot.org/uniprot/ACRB_ECOLI ACRB_ECOLI] AcrAB is a drug efflux protein with a broad substrate specificity.<ref>PMID:16915237</ref> <ref>PMID:16946072</ref> <ref>PMID:17194213</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Membrane proteins function in native cell membranes, but extraction into isolated particles is needed for many biochemical and structural analyses. Commonly used detergent-extraction methods destroy naturally associated lipid bilayers. Here, we devised a detergent-free method for preparing cell-membrane nanoparticles to study the multidrug exporter AcrB, by cryo-EM at 3.2-A resolution. We discovered a remarkably well-organized lipid-bilayer structure associated with transmembrane domains of the AcrB trimer. This bilayer patch comprises 24 lipid molecules; inner leaflet chains are packed in a hexagonal array, whereas the outer leaflet has highly irregular but ordered packing. Protein side chains interact with both leaflets and participate in the hexagonal pattern. We suggest that the lipid bilayer supports and harmonizes peristaltic motions through AcrB trimers. In AcrB D407A, a putative proton-relay mutant, lipid bilayer buttresses protein interactions lost in crystal structures after detergent-solubilization. Our detergent-free system preserves lipid-protein interactions for visualization and should be broadly applicable.
 
Structure and activity of lipid bilayer within a membrane-protein transporter.,Qiu W, Fu Z, Xu GG, Grassucci RA, Zhang Y, Frank J, Hendrickson WA, Guo Y Proc Natl Acad Sci U S A. 2018 Dec 3. pii: 1812526115. doi:, 10.1073/pnas.1812526115. PMID:30509977<ref>PMID:30509977</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6csx" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Ecoli]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Fu, Z]]
[[Category: Fu Z]]
[[Category: Guo, Y]]
[[Category: Guo Y]]
[[Category: Qiu, W]]
[[Category: Qiu W]]
[[Category: Acrb]]
[[Category: Lipid bilayer]]
[[Category: Native cell membrane nanoparticle]]
[[Category: Sma]]
[[Category: Transport protein]]

Latest revision as of 17:30, 13 March 2024

Single particles Cryo-EM structure of AcrB D407A associated with lipid bilayer at 3.0 AngstromSingle particles Cryo-EM structure of AcrB D407A associated with lipid bilayer at 3.0 Angstrom

6csx, resolution 3.00Å

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