3LRB

Structure of E. coli AdiC

「3H5M」から置き換えられました

3LRB の概要

• エントリーDOI: 10.2210/pdb3lrb/pdb
• 関連するPDBエントリー: 3LRC
• 分子名称: Arginine/agmatine antiporter (1 entity in total)
• 機能のキーワード: transporter, antiporter, adic, amino-acid transport, antiport, cell inner membrane, cell membrane, membrane, transmembrane, transport, transport protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein (By similarity): P60063
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 93738.52

構造登録者

Gao, X.,Lu, F.,Zhou, L.,Shi, Y. (登録日: 2010-02-10, 公開日: 2010-02-23, 最終更新日: 2024-03-20)

主引用文献

Gao, X.,Lu, F.,Zhou, L.,Dang, S.,Sun, L.,Li, X.,Wang, J.,Shi, Y.
Structure and mechanism of an amino acid antiporter
Science, 324:1565-1568, 2009

PubMed Abstract: 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 A 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.

PubMed: 19478139
DOI: 10.1126/science.1173654

実験手法

X-RAY DIFFRACTION (3.61 Å)