Despite their major importance in biology and medicine, so far the atomic structure of only a few ABC transporters has been decoded. Now, under the supervision of Markus Seeger and Professor Markus Grütter, PhD student Michael Hohl and senior scientist Christophe Briand have succeeded in cracking the atomic structure of the new ABC transporter "TM287/288".
The membrane protein originates from a thermophilic bacterium. Compared to structures already known, "TM287/288" has two different protein chains that assemble into a heterodimer. About half of the 40 human ABC transporters are heterodimers. "The asymmetries discovered enable us to consider the role of ABC transporters in a new light," explains Seeger. "In the longer term, our results could help develop new medication against multi-resistant bacteria or tumors that are difficult to treat. They also make new approaches to curing or alleviating hereditary diseases possible," concludes Grütter.
Michael Hohl, Christophe Briand, Markus G. Grütter & Markus A. Seeger. Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation. In: Nature Structural & Molecular Biology, March 28, 2012. Doi: 10.1038/nsmb.2267
University of Zurich
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