4u96: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "4u96" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
''' | ==Coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump AcrB== | ||
<StructureSection load='4u96' size='340' side='right' caption='[[4u96]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4u96]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U96 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U96 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</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=4u96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u96 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u96 RCSB], [http://www.ebi.ac.uk/pdbsum/4u96 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Membrane transporters of the RND superfamily confer multidrug resistance to pathogenic bacteria, and are essential for cholesterol metabolism and embryonic development in humans. We use high-resolution X-ray crystallography and computational methods to delineate the mechanism of the homotrimeric RND-type proton/drug antiporter AcrB, the active component of the major efflux system AcrAB-TolC in Escherichia coli, and one most complex and intriguing membrane transporters known to date. Analysis of wildtype AcrB and four functionally-inactive variants reveals an unprecedented mechanism that involves two remote alternating-access conformational cycles within each protomer, namely one for protons in the transmembrane region and another for drugs in the periplasmic domain, 50 A apart. Each of these cycles entails two distinct types of collective motions of two structural repeats, coupled by flanking alpha-helices that project from the membrane. Moreover, we rationalize how the cross-talk among protomers across the trimerization interface might lead to a more kinetically efficient efflux system. | |||
Coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump AcrB.,Eicher T, Seeger MA, Anselmi C, Zhou W, Brandstatter L, Verrey F, Diederichs K, Faraldo-Gomez JD, Pos KM Elife. 2014 Sep 19;3. doi: 10.7554/eLife.03145. PMID:25248080<ref>PMID:25248080</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Pos, K M.]] | |||
[[Category: Darpin]] | |||
[[Category: Membrane protein]] | |||
[[Category: Multidrug efflux protein]] | |||
[[Category: Transport protein]] | |||
Revision as of 11:50, 22 October 2014
Coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump AcrB
| ||||||||||||
