Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters

被引：103

作者：

Quistgaard, Esben M. ^{[1
]}

Low, Christian ^{[1
]}

Moberg, Per ^{[1
]}

Tresaugues, Lionel ^{[1
]}

Nordlund, Par ^{[1
,2
]}

机构：

[1] Karolinska Inst, Dept Med Biochem & Biophys, Stockholm, Sweden

[2] Nanyang Technol Univ, Sch Biol Sci, Singapore 639798, Singapore

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2013年 / 20卷 / 06期

基金：

瑞典研究理事会; 新加坡国家研究基金会;

关键词：

CRYSTAL-STRUCTURE; MECHANISM; SEQUENCE; MODEL;

D O I：

10.1038/nsmb.2569

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：

Here we present two structures of the major facilitator (MFS) xylose transporter XylE from Escherichia coli in inward open and partially occluded inward open conformations. These structures provide key information about the transport cycle of XylE and the closely related human GLUT transporters. This is, to our knowledge, the first MFS transporter structure determined in more than one conformational state, which may establish XylE as an important MFS model protein.

引用

页码：766 / +

页数：4

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