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| | ==Structure of E. coli AdiC (P1)== | | ==Structure of E. coli AdiC (P1)== |
| - | <StructureSection load='3lrc' size='340' side='right' caption='[[3lrc]], [[Resolution|resolution]] 4.00Å' scene=''> | + | <StructureSection load='3lrc' size='340' side='right'caption='[[3lrc]], [[Resolution|resolution]] 4.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3lrc]] is a 4 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=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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LRC FirstGlance]. <br> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lrb|3lrb]]</td></tr> | + | </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='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'>[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> |
| - | <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=3lrc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lrc OCA], [http://pdbe.org/3lrc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lrc RCSB], [http://www.ebi.ac.uk/pdbsum/3lrc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lrc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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. | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Eco57]] | + | [[Category: Escherichia coli O157:H7]] |
| - | [[Category: Gao, X]] | + | [[Category: Large Structures]] |
| - | [[Category: Lu, F]] | + | [[Category: Gao X]] |
| - | [[Category: Shi, Y]] | + | [[Category: Lu F]] |
| - | [[Category: Zhou, L]] | + | [[Category: Shi Y]] |
| - | [[Category: Adic]]
| + | [[Category: Zhou L]] |
| - | [[Category: Amino-acid transport]]
| + | |
| - | [[Category: Antiport]]
| + | |
| - | [[Category: Antiporter]]
| + | |
| - | [[Category: Cell inner membrane]]
| + | |
| - | [[Category: Cell membrane]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Transporter]]
| + | |
| Structural highlights
Function
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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gao X, Lu F, Zhou L, Dang S, Sun L, Li X, Wang J, Shi Y. Structure and mechanism of an amino acid antiporter. Science. 2009 Jun 19;324(5934):1565-8. Epub 2009 May 28. PMID:19478139
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