Structure and Mechanism of an Amino Acid Antiporter

被引：188

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

页码：1565 / 1568

页数：4

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