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TitleHigh-resolution structure of the amino acid transporter AdiC reveals insights into the role of water molecules and networks in oligomerization and substrate binding.
Journal, issue, pagesBmc Biol., Vol. 19, Page 179-179, Year 2021
Publish dateApr 14, 2021 (structure data deposition date)
AuthorsIlgu, H. / Jeckelmann, J.M. / Kalbermatter, D. / Ucurum, Z. / Lemmin, T. / Fotiadis, D.
External linksBmc Biol. / PubMed:34461897
MethodsX-ray diffraction
Resolution1.69 Å
Structure data

PDB-7o82:
The L-arginine/agmatine antiporter from E. coli at 1.7 A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.69 Å

Chemicals

ChemComp-BNG:
nonyl beta-D-glucopyranoside / detergent*YM

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-HEX:
HEXANE

ChemComp-D10:
DECANE

ChemComp-OCT:
N-OCTANE

ChemComp-HOH:
WATER

Source
  • escherichia coli o157:h7 (bacteria)
KeywordsTRANSPORT PROTEIN / AdiC / Transporter / Membrane Protein

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