Enzymes
| UniProtKB help_outline | 2 proteins |
Reaction participants Show >> << Hide
- Name help_outline D-galactonate Identifier CHEBI:12931 Charge -1 Formula C6H11O7 InChIKeyhelp_outline RGHNJXZEOKUKBD-MGCNEYSASA-M SMILEShelp_outline OC[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:29835 | RHEA:29836 | RHEA:29837 | RHEA:29838 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Structures suggest a mechanism for energy coupling by a family of organic anion transporters.
Leano J.B., Batarni S., Eriksen J., Juge N., Pak J.E., Kimura-Someya T., Robles-Colmenares Y., Moriyama Y., Stroud R.M., Edwards R.H.
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 l ... >> More
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. << Less