TY - JOUR
T1 - Structure and mechanism of an amino acid antiporter
AU - Gao, Xiang
AU - Lu, Feiran
AU - Zhou, Lijun
AU - Dang, Shangyu
AU - Sun, Linfeng
AU - Li, Xiaochun
AU - Wang, Jiawei
AU - Shi, Yigong
PY - 2009/6/19
Y1 - 2009/6/19
N2 - 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 Å 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.
AB - 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 Å 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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U2 - 10.1126/science.1173654
DO - 10.1126/science.1173654
M3 - Article
C2 - 19478139
AN - SCOPUS:67649200539
SN - 0036-8075
VL - 324
SP - 1565
EP - 1568
JO - Science
JF - Science
IS - 5934
ER -