Transcriptional activator DmpR – combining biocrystallography and bioinformatics
Uwe H. Sauer, J. Wolf, Günter Stier, Christin Grundström, Victoria Shingler · Acta Crystallographica Section A Foundations of Crystallography · 2011
Sessions C633The concept of the cell as a collection of multi-subunit protein complexes are emerging as a cornerstone of modern biology.Transcription by RNA polymerase II (Pol II) is a prime example for this concept as it is regulated by large protein assemblies comprising many subunits, including Mediator.Structure determination of these multi-protein complexes is essential to understand gene regulation mechanism.We have solved crystal structure of the Mediator Head module (7 subunits, 223 kDa) at 4.3 Å resolution [1].Our Mediator Head structure reveals the striking complex assembly mechanism: the multi-helical bundle with five different Mediator subunits is formed as a single structure unit, thereby ensuring stable assembly of the Head subunits, as well as providing the binding sites for general transcription factors (GTFs) and Pol II.Such interactions could not have been determined from structures of individual subunits alone, or from analyzing pairwise small domain-domain interactions, but only by study of the multiprotein complex in its entirety.