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Maria A. Schumacher

Researcher at Duke University

Publications -  123
Citations -  9022

Maria A. Schumacher is an academic researcher from Duke University. The author has contributed to research in topics: Binding site & Repressor. The author has an hindex of 48, co-authored 123 publications receiving 8250 citations. Previous affiliations of Maria A. Schumacher include Oregon Health & Science University & University of Texas Health Science Center at Houston.

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Crystal structure of the lactose operon repressor and its complexes with DNA and inducer.

TL;DR: In this article, the three-dimensional structures of the intact lac repressor, the Lac repressor bound to the gratuitous inducer isopropyl-β-D-1-thiogalactoside (IPTG), and the lac Repressor complexed with a 21-base pair symmetric operator DNA have been determined.
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Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin.

TL;DR: The crystal structure of the small-conductance Ca2+-activated K+ channels CaMBD/Ca2+/CaM complex is reported and suggests a possible gating mechanism for the SK channel.
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Structures of the pleiotropic translational regulator Hfq and an Hfq–RNA complex: a bacterial Sm‐like protein

TL;DR: The Hfq–RNA structure reveals that the single‐stranded hepta‐oligoribonucleotide binds in a circular conformation around a central basic cleft, whereby Tyr42 residues from adjacent subunits stack with six of the bases, and Gln8, outside the Sm motif, provides key protein–base contacts, which suggests a mechanism for H fq function.
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Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices

TL;DR: The three-dimensional structure of a ternary complex of the purine repressor, PurR, bound to both its corepressor, hypoxanthine, and the 16-base pair purF operator site has been solved at 2.7 A resolution by x-ray crystallography.
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Structural Mechanisms of QacR Induction and Multidrug Recognition

TL;DR: The Staphylococcus aureus multidrug binding protein QacR represses transcription of the qacA multi-drug transporter gene and is induced by structurally diverse cationic lipophilic drugs as discussed by the authors.