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3lrc

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{{Seed}}
 
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[[Image:3lrc.jpg|left|200px]]
 
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==Structure of E. coli AdiC (P1)==
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The line below this paragraph, containing "STRUCTURE_3lrc", creates the "Structure Box" on the page.
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<StructureSection load='3lrc' size='340' side='right'caption='[[3lrc]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3lrc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3h6b 3h6b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LRC FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.004&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lrc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lrc OCA], [https://pdbe.org/3lrc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lrc RCSB], [https://www.ebi.ac.uk/pdbsum/3lrc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lrc ProSAT]</span></td></tr>
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{{STRUCTURE_3lrc| PDB=3lrc | SCENE= }}
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</table>
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== Function ==
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[https://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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lr/3lrc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=3lrc ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Structure of E. coli AdiC (P1)===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_19478139}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3lrc" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19478139 is the PubMed ID number.
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== References ==
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-->
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<references/>
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{{ABSTRACT_PUBMED_19478139}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia coli O157:H7]]
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3LRC is a 4 chains structure with sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3h6b 3h6b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LRC OCA].
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[[Category: Large Structures]]
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[[Category: Gao X]]
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==Reference==
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[[Category: Lu F]]
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<ref group="xtra">PMID:19478139</ref><references group="xtra"/>
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[[Category: Shi Y]]
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[[Category: Escherichia coli]]
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[[Category: Zhou L]]
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[[Category: Gao, X.]]
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[[Category: Lu, F.]]
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[[Category: Shi, Y.]]
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[[Category: Zhou, L.]]
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[[Category: Adic]]
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[[Category: Amino-acid transport]]
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[[Category: Antiport]]
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[[Category: Antiporter]]
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[[Category: Cell inner membrane]]
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[[Category: Cell membrane]]
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[[Category: Membrane]]
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[[Category: Transmembrane]]
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[[Category: Transport]]
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[[Category: Transport protein]]
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[[Category: Transporter]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 25 13:22:55 2010''
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Current revision

Structure of E. coli AdiC (P1)

PDB ID 3lrc

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