4djk: Difference between revisions
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[[ | ==Structure of glutamate-GABA antiporter GadC== | ||
<StructureSection load='4djk' size='340' side='right' caption='[[4djk]], [[Resolution|resolution]] 3.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4djk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DJK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DJK FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dji|4dji]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gadC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=4djk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4djk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4djk RCSB], [http://www.ebi.ac.uk/pdbsum/4djk PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Food-borne hemorrhagic Escherichia coli, exemplified by the strains O157:H7 and O104:H4 (refs 1, 2), require elaborate acid-resistance systems (ARs) to survive the extremely acidic environment such as the stomach (pH approximately 2). AR2 expels intracellular protons through the decarboxylation of L-glutamate (Glu) in the cytoplasm and exchange of the reaction product gamma-aminobutyric acid (GABA) with extracellular Glu. The latter process is mediated by the Glu-GABA antiporter GadC, a representative member of the amino-acid-polyamine-organocation superfamily of membrane transporters. The functional mechanism of GadC remains largely unknown. Here we show, with the use of an in vitro proteoliposome-based assay, that GadC transports GABA/Glu only under acidic conditions, with no detectable activity at pH values higher than 6.5. We determined the crystal structure of E. coli GadC at 3.1 A resolution under basic conditions. GadC, comprising 12 transmembrane segments (TMs), exists in a closed state, with its carboxy-terminal domain serving as a plug to block an otherwise inward-open conformation. Structural and biochemical analyses reveal the essential transport residues, identify the transport path and suggest a conserved transport mechanism involving the rigid-body rotation of a helical bundle for GadC and other amino acid antiporters. | |||
Structure and mechanism of a glutamate-GABA antiporter.,Ma D, Lu P, Yan C, Fan C, Yin P, Wang J, Shi Y Nature. 2012 Mar 11;483(7391):632-6. doi: 10.1038/nature10917. PMID:22407317<ref>PMID:22407317</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Fan, C | [[Category: Fan, C]] | ||
[[Category: Lu, P L | [[Category: Lu, P L]] | ||
[[Category: Ma, D | [[Category: Ma, D]] | ||
[[Category: Shi, Y G | [[Category: Shi, Y G]] | ||
[[Category: Wang, J W | [[Category: Wang, J W]] | ||
[[Category: Yan, C Y | [[Category: Yan, C Y]] | ||
[[Category: Yin, P | [[Category: Yin, P]] | ||
[[Category: Glutamate-gaba antiporter]] | [[Category: Glutamate-gaba antiporter]] | ||
[[Category: Leut]] | [[Category: Leut]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
Revision as of 13:23, 4 January 2015
Structure of glutamate-GABA antiporter GadC
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