7nb6

<table><tr><td colspan='2'>[[7nb6]] is a 5 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=7NB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NB6 FirstGlance]. <br>

</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=7nb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nb6 OCA], [https://pdbe.org/7nb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nb6 RCSB], [https://www.ebi.ac.uk/pdbsum/7nb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nb6 ProSAT]</span></td></tr>

== Function ==

[[https://www.uniprot.org/uniprot/TQSA_ECOLI TQSA_ECOLI]] Controls the transport of the quorum-sensing signal AI-2 either by enhancing its secretion or inhibiting its uptake and consequently represses biofilm formation and motility and affects the global gene expression in biofilms.<ref>PMID:16385049</ref>

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== Publication Abstract from PubMed ==

Bacteria utilize small extracellular molecules to communicate in order to collectively coordinate their behaviors in response to the population density. Autoinducer-2 (AI-2), a universal molecule for both intra- and inter-species communication, is involved in the regulation of biofilm formation, virulence, motility, chemotaxis, and antibiotic resistance. While many studies have been devoted to understanding the biosynthesis and sensing of AI-2, very little information is available on its export. The protein TqsA from Escherichia coli, which belongs to the AI-2 exporter superfamily, has been shown to export AI-2. Here, we report the cryogenic electron microscopic structures of two AI-2 exporters (TqsA and YdiK) from E. coli at 3.35 A and 2.80 A resolutions, respectively. Our structures suggest that the AI-2 exporter exists as a homo-pentameric complex. In silico molecular docking and native mass spectrometry experiments were employed to demonstrate the interaction between AI-2 and TqsA, and the results highlight the functional importance of two helical hairpins in substrate binding. We propose that each monomer works as an independent functional unit utilizing an elevator-type transport mechanism.

Cryo-EM structures of pentameric autoinducer-2 exporter from Escherichia coli reveal its transport mechanism.,Khera R, Mehdipour AR, Bolla JR, Kahnt J, Welsch S, Ermler U, Muenke C, Robinson CV, Hummer G, Xie H, Michel H EMBO J. 2022 Jun 14:e109990. doi: 10.15252/embj.2021109990. PMID:35698912<ref>PMID:35698912</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Escherichia coli K-12]]