Electron and atomic force microscopy of the trimeric ammonium transporter AmtB

被引：39

作者：

Conroy, MJ

Jamieson, SJ

Blakey, D

Kaufmann, T

Engel, A

Fotiadis, D

Merrick, M

Bullough, PA

机构：

[1] Univ Sheffield, Krebs Inst Biomol Res, Dept Mol Biol & Biotechnol, Sheffield S10 2TN, S Yorkshire, England

[2] John Innes Ctr Plant Sci Res, Dept Mol Microbiol, Norwich NR4 7UH, Norfolk, England

[3] Univ Basel, Bioctr, ME Muller Inst Struct Biol, CH-4056 Basel, Switzerland

来源：

EMBO REPORTS | 2004年 / 5卷 / 12期

基金：

英国生物技术与生命科学研究理事会;

关键词：

atomic force microscopy; electron microscopy; membrane protein; ammonium transport; projection structure;

D O I：

10.1038/sj.embor.7400296

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Escherichia coli AmtB is an archetypal member of the ammonium transporter (Amt) family, a family of proteins that are conserved in all domains of life. Reconstitution of AmtB in the presence of lipids produced large, ordered two-dimensional crystals. From these, a 12 Angstrom resolution projection map was determined by cryoelectron microscopy, and high-resolution topographs were acquired using atomic force microscopy. Both techniques showed the trimeric structure of AmtB in which each monomer seems to have a pseudo-two-fold symmetry. This arrangement is likely to represent the in vivo structure. This work provides the first views of the structure of any member of the Amt family.

引用

页码：1153 / 1158

页数：6

共 32 条

[1] Structure and mechanism of the lactose permease of Escherichia coli [J].