3lrc
From Proteopedia
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| - | {{STRUCTURE_3lrc| PDB=3lrc | SCENE= }} | ||
| - | ===Structure of E. coli AdiC (P1)=== | ||
| - | {{ABSTRACT_PUBMED_19478139}} | ||
| - | == | + | ==Structure of E. coli AdiC (P1)== |
| - | [[http://www.uniprot.org/uniprot/ADIC_ECO57 ADIC_ECO57 | + | <StructureSection load='3lrc' size='340' side='right'caption='[[3lrc]], [[Resolution|resolution]] 4.00Å' scene=''> |
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.004Å</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=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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lr/3lrc_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| - | [[Category: Escherichia coli]] | + | <div class="pdbe-citations 3lrc" style="background-color:#fffaf0;"></div> |
| - | [[Category: Gao | + | == References == |
| - | [[Category: Lu | + | <references/> |
| - | [[Category: Shi | + | __TOC__ |
| - | [[Category: Zhou | + | </StructureSection> |
| - | + | [[Category: Escherichia coli O157:H7]] | |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Gao X]] | |
| - | + | [[Category: Lu F]] | |
| - | + | [[Category: Shi Y]] | |
| - | + | [[Category: Zhou L]] | |
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Current revision
Structure of E. coli AdiC (P1)
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