Structure and Mechanism of an Amino Acid Antiporter

被引：186
作者：
Gao, Xiang [1 ,2 ]
Lu, Feiran [1 ,2 ]
Zhou, Lijun [1 ,2 ]
Dang, Shangyu [1 ,2 ]
Sun, Linfeng [1 ,2 ]
Li, Xiaochun [1 ,2 ]
Wang, Jiawei [1 ,2 ]
Shi, Yigong [1 ,3 ]
机构：
[1] Tsinghua Univ, Struct Biol Ctr, Dept Biol Sci & Biotechol, Beijing 100084, Peoples R China
[2] Tsinghua Univ, State Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R China
[3] Tsinghua Univ, Sch Med, Beijing 100084, Peoples R China
来源：
SCIENCE | 2009年 / 324卷 / 5934期
关键词：
ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; TRANSPORTER SUPERFAMILY; AGMATINE ANTIPORTER; RECOGNITION SITE; MOLECULAR-BASIS; RESISTANCE; PUTRESCINE; EXCRETION; ARGININE;
D O I：
10.1126/science.1173654
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
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.
引用
收藏
页码：1565 / 1568
页数：4
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