6E9O

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

Summary for 6E9O

• Entry DOI: 10.2210/pdb6e9o/pdb
• Related: 6E9N
• Descriptor: D-galactonate transport, D-galactonic acid (3 entities in total)
• Functional Keywords: mfs transporter, slc17, organic anion transporter, membrane protein
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 101397.06

Authors

Leano, J.B.,Edwards, R.H.,Stroud, R.M. (deposition date: 2018-08-01, release date: 2019-05-22, Last modification date: 2023-10-11)

Primary citation

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.
Structures suggest a mechanism for energy coupling by a family of organic anion transporters.
Plos Biol., 17:e3000260-e3000260, 2019

PubMed Abstract: 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.

PubMed: 31083648
DOI: 10.1371/journal.pbio.3000260

Experimental method

X-RAY DIFFRACTION (3.501 Å)