7O82

The L-arginine/agmatine antiporter from E. coli at 1.7 A resolution

Summary for 7O82

• Entry DOI: 10.2210/pdb7o82/pdb
• Descriptor: Arginine/agmatine antiporter, nonyl beta-D-glucopyranoside, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (7 entities in total)
• Functional Keywords: adic, transporter, membrane protein, transport protein
• Biological source: Escherichia coli O157:H7
• Total number of polymer chains: 2
• Total formula weight: 97762.09

Authors

Jeckelmann, J.M.,Ilgue, H.,Kalbermatter, D.,Fotiadis, D. (deposition date: 2021-04-14, release date: 2021-09-08, Last modification date: 2024-01-31)

Primary citation

Ilgu, H.,Jeckelmann, J.M.,Kalbermatter, D.,Ucurum, Z.,Lemmin, T.,Fotiadis, D.
High-resolution structure of the amino acid transporter AdiC reveals insights into the role of water molecules and networks in oligomerization and substrate binding.
Bmc Biol., 19:179-179, 2021

PubMed Abstract: The L-arginine/agmatine transporter AdiC is part of the arginine-dependent extreme acid resistance system of the bacterium Escherichia coli and its pathogenic varieties such as strain E. coli O157:H7. At the present time, there is a lack of knowledge concerning the role of water molecules and networks for the structure and function of AdiC, and solute transporters in general.

PubMed: 34461897
DOI: 10.1186/s12915-021-01102-4

Experimental method

X-RAY DIFFRACTION (1.69 Å)