3lrb

<StructureSection load='3lrb' size='340' side='right' caption='[[3lrb]], [[Resolution|resolution]] 3.61&Aring;' scene=''>

<table><tr><td colspan='2'>[[3lrb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3h5m 3h5m]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LRB FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lrc|3lrc]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">adiC, Z5717, ECs5097 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</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=3lrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lrb OCA], [http://pdbe.org/3lrb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lrb RCSB], [http://www.ebi.ac.uk/pdbsum/3lrb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lrb ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/ADIC_ECO57 ADIC_ECO57]] Major component of the acid-resistance (AR) system allowing enteric pathogens to survive the acidic environment in the stomach. Exchanges extracellular arginine for its intracellular decarboxylation product agmatine (Agm) thereby expelling intracellular protons.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lr/3lrb_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

Virulent enteric pathogens such as Escherichia coli strain O157:H7 rely on acid-resistance (AR) systems to survive the acidic environment in the stomach. A major component of AR is an arginine-dependent arginine:agmatine antiporter that expels intracellular protons. Here, we report the crystal structure of AdiC, the arginine:agmatine antiporter from E. coli O157:H7 and a member of the amino acid/polyamine/organocation (APC) superfamily of transporters at 3.6 A resolution. The overall fold is similar to that of several Na+-coupled symporters. AdiC contains 12 transmembrane segments, forms a homodimer, and exists in an outward-facing, open conformation in the crystals. A conserved, acidic pocket opens to the periplasm. Structural and biochemical analysis reveals the essential ligand-binding residues, defines the transport route, and suggests a conserved mechanism for the antiporter activity.

Structure and mechanism of an amino acid antiporter.,Gao X, Lu F, Zhou L, Dang S, Sun L, Li X, Wang J, Shi Y Science. 2009 Jun 19;324(5934):1565-8. Epub 2009 May 28. PMID:19478139<ref>PMID:19478139</ref>

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

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<div class="pdbe-citations 3lrb" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Eco57]]

[[Category: Gao, X]]

[[Category: Lu, F]]

[[Category: Shi, Y]]

[[Category: Zhou, L]]

[[Category: Transporter]]