6e9o

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E. coli D-galactonate:proton symporter mutant E133Q in the outward substrate-bound form

Structural highlights

6e9o is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.501Å
Ligands:J0M
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

J7QAK3_ECOLX

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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See Also

References

  1. Leano JB, Batarni S, Eriksen J, Juge N, Pak JE, Kimura-Someya T, Robles-Colmenares Y, Moriyama Y, Stroud RM, Edwards RH. Structures suggest a mechanism for energy coupling by a family of organic anion transporters. PLoS Biol. 2019 May 13;17(5):e3000260. doi: 10.1371/journal.pbio.3000260. PMID:31083648 doi:http://dx.doi.org/10.1371/journal.pbio.3000260

Contents


PDB ID 6e9o

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