Journal
SCIENCE
Volume 324, Issue 5934, Pages 1565-1568Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1173654
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Funding
- Ministry of Science and Technology [2009CB918801]
- Tsinghua University 985 Phase II
- National Natural Science Foundation
- Beijing Municipal Commissions of Education and Science and Technology
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Virulent enteric pathogens such as Escherichia coli strain O157:H7 rely on acid-resistance (AR) systems to survive the acidic environment in the stomach. A major component of AR is an arginine-dependent arginine: agmatine antiporter that expels intracellular protons. Here, we report the crystal structure of AdiC, the arginine: agmatine antiporter from E. coli O157:H7 and a member of the amino acid/polyamine/organocation (APC) superfamily of transporters at 3.6 angstrom resolution. The overall fold is similar to that of several Na+-coupled symporters. AdiC contains 12 transmembrane segments, forms a homodimer, and exists in an outward-facing, open conformation in the crystals. A conserved, acidic pocket opens to the periplasm. Structural and biochemical analysis reveals the essential ligand-binding residues, defines the transport route, and suggests a conserved mechanism for the antiporter activity.
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