5nc5: Difference between revisions

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'''Unreleased structure'''


The entry 5nc5 is ON HOLD
==Crystal structure of AcrBZ in complex with antibiotic puromycin==
<StructureSection load='5nc5' size='340' side='right' caption='[[5nc5]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nc5]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NC5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NC5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=D12:DODECANE'>D12</scene>, <scene name='pdbligand=DD9:NONANE'>DD9</scene>, <scene name='pdbligand=HEX:HEXANE'>HEX</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=PUY:PUROMYCIN'>PUY</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=5nc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nc5 OCA], [http://pdbe.org/5nc5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nc5 RCSB], [http://www.ebi.ac.uk/pdbsum/5nc5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nc5 ProSAT]</span></td></tr>
</table>
== 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>  [[http://www.uniprot.org/uniprot/ACRZ_ECO57 ACRZ_ECO57]] AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with a broad substrate specificity. This protein binds to AcrB and is required for efflux of some but not all substrates, suggesting it may influence the specificity of drug export.[HAMAP-Rule:MF_01484]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial efflux pumps confer multidrug resistance by transporting diverse antibiotics from the cell. In Gram-negative bacteria, some of these pumps form multi-protein assemblies that span the cell envelope. Here we report the near-atomic resolution cryoEM structures of the Escherichia coli AcrAB-TolC multidrug efflux pump in resting and drug transport states, revealing a quaternary structural switch that allosterically couples and synchronizes initial ligand binding with channel opening. Within the transport-activated state, the channel remains open even though the pump cycles through three distinct conformations. Collectively, our data provide a dynamic mechanism for the assembly and operation of the AcrAB-TolC pump.


Authors: Du, D., Luisi, B.
An allosteric transport mechanism for the AcrAB-TolC Multidrug Efflux Pump.,Wang Z, Fan G, Hryc CF, Blaza JN, Serysheva II, Schmid MF, Chiu W, Luisi BF, Du D Elife. 2017 Mar 29;6. pii: e24905. doi: 10.7554/eLife.24905. PMID:28355133<ref>PMID:28355133</ref>


Description: Crystal structure of AcrBZ in complex with antibiotic puromycin
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5nc5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Du, D]]
[[Category: Luisi, B]]
[[Category: Luisi, B]]
[[Category: Du, D]]
[[Category: Membrane transporter]]
[[Category: Multidrug efflux pump]]
[[Category: Transport protein]]
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