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Trends Biochem Sci. 2013 Mar;38(3):151-9. doi: 10.1016/j.tibs.2013.01.003. Epub 2013 Feb 8.

Structural advances for the major facilitator superfamily (MFS) transporters.

Author information

1
State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Medicine, Tsinghua-Peking Center for Life Sciences, Tsinghua University, Beijing 100084, China. nyan@tsinghua.edu.cn

Abstract

The major facilitator superfamily (MFS) is one of the largest groups of secondary active transporters conserved from bacteria to humans. MFS proteins selectively transport a wide spectrum of substrates across biomembranes and play a pivotal role in multiple physiological processes. Despite intense investigation, only seven MFS proteins from six subfamilies have been structurally elucidated. These structures were captured in distinct states during a transport cycle involving alternating access to binding sites from either side of the membrane. This review discusses recent progress in MFS structure analysis and focuses on the molecular basis for substrate binding, co-transport coupling, and alternating access.

PMID:
23403214
DOI:
10.1016/j.tibs.2013.01.003
[Indexed for MEDLINE]

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