Projection structure and molecular architecture of OxIT, a bacterial membrane transporter

被引:52
作者
Heymann, JAW
Sarker, R
Hirai, T
Shi, D
Milne, JLS
Maloney, PC
Subramaniam, S [1 ]
机构
[1] NCI, Biochem Lab, NIH, Bethesda, MD 20892 USA
[2] NCI, Cell Biol Lab, NIH, Bethesda, MD 20892 USA
[3] Johns Hopkins Univ, Sch Med, Dept Physiol, Baltimore, MD 21205 USA
关键词
electron cryo-microscopy; major facilitator superfamily; membrane transporter; two-dimensional crystallization;
D O I
10.1093/emboj/20.16.4408
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
The major facilitator superfamily (MFS) represents the largest collection of evolutionarily related members within the class of membrane 'carrier' proteins. OAT, a representative example of the MFS, is an oxalate-transporting membrane protein in Oxalobacter formigenes. From an electron crystallographic analysis of two-dimensional crystals of OAT, we have determined the projection structure of this membrane transporter. The projection map at 6 Angstrom resolution indicates the presence of 12 transmembrane helices in each monomer of OxlT, with one set of six helices related to the other set by an approximate internal two-fold axis. The projection map reveals the existence of a central cavity, which we propose to be part of the pathway of oxalate transport. By combining information from the projection map with related biochemical data, we present probable models for the architectural arrangement of transmembrane helices in this protein superfamily.
引用
收藏
页码:4408 / 4413
页数:6
相关论文
共 24 条