6e9o: Difference between revisions
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==E. coli D-galactonate:proton symporter mutant E133Q in the outward substrate-bound form== | |||
<StructureSection load='6e9o' size='340' side='right'caption='[[6e9o]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6e9o]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E9O FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=J0M:D-galactonic+acid'>J0M</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6e9n|6e9n]]</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=6e9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e9o OCA], [http://pdbe.org/6e9o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e9o RCSB], [http://www.ebi.ac.uk/pdbsum/6e9o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e9o ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Members of the solute carrier 17 (SLC17) family use divergent mechanisms to concentrate organic anions. Membrane potential drives uptake of the principal excitatory neurotransmitter glutamate into synaptic vesicles, whereas closely related proteins use proton cotransport to drive efflux from the lysosome. To delineate the divergent features of ionic coupling by the SLC17 family, we determined the structure of Escherichia coli D-galactonate/H+ symporter D-galactonate transporter (DgoT) in 2 states: one open to the cytoplasmic side and the other open to the periplasmic side with substrate bound. The structures suggest a mechanism that couples H+ flux to substrate recognition. A transition in the role of H+ from flux coupling to allostery may confer regulation by trafficking to and from the plasma membrane. | |||
Structures suggest a mechanism for energy coupling by a family of organic anion transporters.,Leano JB, Batarni S, Eriksen J, Juge N, Pak JE, Kimura-Someya T, Robles-Colmenares Y, Moriyama Y, Stroud RM, Edwards RH PLoS Biol. 2019 May 13;17(5):e3000260. doi: 10.1371/journal.pbio.3000260. PMID:31083648<ref>PMID:31083648</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Leano, J | <div class="pdbe-citations 6e9o" style="background-color:#fffaf0;"></div> | ||
[[Category: Stroud, R | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Edwards, R H]] | |||
[[Category: Leano, J B]] | |||
[[Category: Stroud, R M]] | |||
[[Category: Membrane protein]] | |||
[[Category: Mfs transporter]] | |||
[[Category: Organic anion transporter]] | |||
[[Category: Slc17]] | |||
Revision as of 09:44, 23 May 2019
E. coli D-galactonate:proton symporter mutant E133Q in the outward substrate-bound formE. coli D-galactonate:proton symporter mutant E133Q in the outward substrate-bound form
Structural highlights
Publication Abstract from PubMedMembers of the solute carrier 17 (SLC17) family use divergent mechanisms to concentrate organic anions. Membrane potential drives uptake of the principal excitatory neurotransmitter glutamate into synaptic vesicles, whereas closely related proteins use proton cotransport to drive efflux from the lysosome. To delineate the divergent features of ionic coupling by the SLC17 family, we determined the structure of Escherichia coli D-galactonate/H+ symporter D-galactonate transporter (DgoT) in 2 states: one open to the cytoplasmic side and the other open to the periplasmic side with substrate bound. The structures suggest a mechanism that couples H+ flux to substrate recognition. A transition in the role of H+ from flux coupling to allostery may confer regulation by trafficking to and from the plasma membrane. Structures suggest a mechanism for energy coupling by a family of organic anion transporters.,Leano JB, Batarni S, Eriksen J, Juge N, Pak JE, Kimura-Someya T, Robles-Colmenares Y, Moriyama Y, Stroud RM, Edwards RH PLoS Biol. 2019 May 13;17(5):e3000260. doi: 10.1371/journal.pbio.3000260. PMID:31083648[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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