2hrt: Difference between revisions
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< | ==Asymmetric structure of trimeric AcrB from Escherichia coli== | ||
<StructureSection load='2hrt' size='340' side='right'caption='[[2hrt]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2hrt]] is a 6 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=2HRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HRT 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]] 3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</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=2hrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hrt OCA], [https://pdbe.org/2hrt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hrt RCSB], [https://www.ebi.ac.uk/pdbsum/2hrt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hrt ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hr/2hrt_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hrt ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The AcrA/AcrB/TolC complex spans the inner and outer membranes of Escherichia coli and serves as its major drug-resistance pump. Driven by the proton motive force, it mediates the efflux of bile salts, detergents, organic solvents, and many structurally unrelated antibiotics. Here, we report a crystallographic structure of trimeric AcrB determined at 2.9 and 3.0 angstrom resolution in space groups that allow asymmetry of the monomers. This structure reveals three different monomer conformations representing consecutive states in a transport cycle. The structural data imply an alternating access mechanism and a novel peristaltic mode of drug transport by this type of transporter. | |||
Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism.,Seeger MA, Schiefner A, Eicher T, Verrey F, Diederichs K, Pos KM Science. 2006 Sep 1;313(5791):1295-8. PMID:16946072<ref>PMID:16946072</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2hrt" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | |||
[[Category: Diederichs K]] | |||
== | [[Category: Eicher T]] | ||
[[Category: Pos KM]] | |||
[[Category: Escherichia coli]] | [[Category: Schiefner A]] | ||
[[Category: | [[Category: Seeger MA]] | ||
[[Category: Diederichs | [[Category: Verrey F]] | ||
[[Category: Eicher | |||
[[Category: Pos | |||
[[Category: Schiefner | |||
[[Category: Seeger | |||
[[Category: Verrey | |||
Latest revision as of 13:01, 30 August 2023
Asymmetric structure of trimeric AcrB from Escherichia coliAsymmetric structure of trimeric AcrB from Escherichia coli
Structural highlights
FunctionACRB_ECOLI AcrAB is a drug efflux protein with a broad substrate specificity.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe AcrA/AcrB/TolC complex spans the inner and outer membranes of Escherichia coli and serves as its major drug-resistance pump. Driven by the proton motive force, it mediates the efflux of bile salts, detergents, organic solvents, and many structurally unrelated antibiotics. Here, we report a crystallographic structure of trimeric AcrB determined at 2.9 and 3.0 angstrom resolution in space groups that allow asymmetry of the monomers. This structure reveals three different monomer conformations representing consecutive states in a transport cycle. The structural data imply an alternating access mechanism and a novel peristaltic mode of drug transport by this type of transporter. Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism.,Seeger MA, Schiefner A, Eicher T, Verrey F, Diederichs K, Pos KM Science. 2006 Sep 1;313(5791):1295-8. PMID:16946072[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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