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2dhh: Difference between revisions

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<StructureSection load='2dhh' size='340' side='right'caption='[[2dhh]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='2dhh' size='340' side='right'caption='[[2dhh]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2dhh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DHH FirstGlance]. <br>
<table><tr><td colspan='2'>[[2dhh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DHH FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2dr6|2dr6]], [[2drd|2drd]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=2dhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dhh OCA], [https://pdbe.org/2dhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dhh RCSB], [https://www.ebi.ac.uk/pdbsum/2dhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dhh 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=2dhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dhh OCA], [https://pdbe.org/2dhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dhh RCSB], [https://www.ebi.ac.uk/pdbsum/2dhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dhh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2dhh ConSurf].
</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=2dhh ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
AcrB is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA. Here we describe crystal structures of AcrB with and without substrates. The AcrB-drug complex consists of three protomers, each of which has a different conformation corresponding to one of the three functional states of the transport cycle. Bound substrate was found in the periplasmic domain of one of the three protomers. The voluminous binding pocket is aromatic and allows multi-site binding. The structures indicate that drugs are exported by a three-step functionally rotating mechanism in which substrates undergo ordered binding change.
Crystal structures of a multidrug transporter reveal a functionally rotating mechanism.,Murakami S, Nakashima R, Yamashita E, Matsumoto T, Yamaguchi A Nature. 2006 Sep 14;443(7108):173-9. Epub 2006 Aug 16. PMID:16915237<ref>PMID:16915237</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2dhh" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Matsumoto, T]]
[[Category: Matsumoto T]]
[[Category: Murakami, S]]
[[Category: Murakami S]]
[[Category: Nakashima, R]]
[[Category: Nakashima R]]
[[Category: Yamashita, E]]
[[Category: Yamashita E]]
[[Category: Antiporter]]
[[Category: Drug resistance]]
[[Category: Exporter]]
[[Category: Membrane protein]]
[[Category: Membrane transporter]]
[[Category: Multidrug efflux]]
[[Category: Transporter]]

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