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Structure paper

TitleNa + -dependent gate dynamics and electrostatic attraction ensure substrate coupling in glutamate transporters.
Journal, issue, pagesSci Adv, Vol. 6, Year 2020
Publish dateSep 24, 2020 (structure data deposition date)
AuthorsAlleva, C. / Kovalev, K. / Astashkin, R. / Berndt, M.I. / Baeken, C. / Balandin, T. / Gordeliy, V. / Fahlke, C. / Machtens, J.P.
External linksSci Adv / PubMed:33208356
MethodsX-ray diffraction
Resolution2.5 Å
Structure data

PDB-7ahk:
Crystal structure of the outward-facing state of the substrate-free Na+-only bound glutamate transporter homolog GltPh
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-BOG:
octyl beta-D-glucopyranoside / detergent*YM

ChemComp-PO4:
PHOSPHATE ION

ChemComp-LFA:
EICOSANE

ChemComp-GOL:
GLYCEROL

ChemComp-OLC:
(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate

ChemComp-HOH:
WATER

Source
  • pyrococcus horikoshii (archaea)
KeywordsMEMBRANE PROTEIN / glutamate transporter / aminoacid transport / homologue

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