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Biochim Biophys Acta Biomembr. 2018 Apr;1860(4):804-808. doi: 10.1016/j.bbamem.2017.08.009. Epub 2017 Aug 31.

Membrane transporter research in times of countless structures.

Author information

1
Institute of Medical Microbiology, University of Zurich, Switzerland. Electronic address: m.seeger@imm.uzh.ch.

Abstract

Structural biology has advanced our understanding of membrane proteins like no other scientific discipline in the past two decades and the number of high resolution membrane transporter structures solved by X-ray crystallography has increased exponentially over this time period. Currently, single particle cryo-EM is in full swing due to a recent resolution revolution and permits for structural insights of proteins that were refractory to crystallization. It is foreseeable that multiple structures of many human transporters will be solved in the coming five years. Nevertheless, many scientifically important questions remain unanswered despite of available structures, as is illustrated in this article at the example of multidrug efflux pumps and ABC transporters. Structure-function studies likely continue to be a supporting pillar of membrane transporter research. However, there is a trend towards the "integrated structural biologist", whose research focusses on a biological question and who closely collaborates with other research groups specialized in spectroscopy techniques or molecular dynamics simulation. Future membrane protein research requires joint efforts from specialists of various disciplines to finally work towards a molecular understanding of membrane transport in the context of the living cell. This article is part of a Special Issue entitled: Beyond the Structure-Function Horizon of Membrane Proteins edited by Ute Hellmich, Rupak Doshi and Benjamin McIlwain.

KEYWORDS:

ABC transporter; Multidrug efflux; Structure-function relationship; The integrated structural biologist

PMID:
28867210
DOI:
10.1016/j.bbamem.2017.08.009
[Indexed for MEDLINE]

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