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Structural advances for the major facilitator superfamily (MFS) transporters

Nieng Yan1

  • 1State 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

Trends in Biochemical Sciences
|February 14, 2013
PubMed

Insights

The major facilitator superfamily (MFS) comprises numerous membrane transport proteins. Recent structural analyses reveal how these transporters bind substrates and move them across membranes.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Transport

Background:

  • The Major Facilitator Superfamily (MFS) is a vast group of secondary active transporters found across all domains of life.
  • MFS proteins are crucial for transporting diverse substrates across biological membranes, impacting numerous physiological functions.
  • Despite their importance, structural information is limited, with only seven MFS proteins from six subfamilies elucidated to date.

Purpose of the Study:

  • To review recent advancements in the structural analysis of MFS proteins.
  • To elucidate the molecular mechanisms underlying substrate binding within MFS transporters.
  • To explore the coupling of co-transport and the alternating access mechanism in MFS proteins.

Main Methods:

  • Analysis of recently determined MFS protein structures.
  • Comparative structural studies across different MFS subfamilies.
  • Molecular modeling and simulation to understand transport dynamics.

Main Results:

  • Structural data reveals distinct conformational states of MFS proteins during transport.
  • Insights into the specific interactions involved in substrate recognition and binding.
  • Elucidation of the alternating access mechanism facilitating transmembrane transport.

Conclusions:

  • Recent structural studies provide a deeper understanding of MFS protein function.
  • The molecular basis for substrate transport and energy coupling is becoming clearer.
  • Further structural investigations will continue to illuminate the diverse roles of MFS transporters.

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