L
Lutz Schmitt
Researcher at University of Düsseldorf
Publications - 202
Citations - 7303
Lutz Schmitt is an academic researcher from University of Düsseldorf. The author has contributed to research in topics: ATP-binding cassette transporter & Secretion. The author has an hindex of 42, co-authored 182 publications receiving 6144 citations. Previous affiliations of Lutz Schmitt include University of Paris & University of Marburg.
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Journal ArticleDOI
Nucleotide dependent monomer/dimer equilibrium of OpuAA, the nucleotide-binding protein of the osmotically regulated ABC transporter OpuA from Bacillus subtilis.
TL;DR: The OpuA system of Bacillus subtilis is a member of the substrate-binding-protein-dependent ABC transporter superfamily and serves for the uptake of the compatible solute glycine betaine under hyperosmotic growth conditions and a model that couples changes in the oligomeric state of OpuAA with ATP hydrolysis is proposed.
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The compatible-solute-binding protein OpuAC from Bacillus subtilis: ligand binding, site-directed mutagenesis, and crystallographic studies.
TL;DR: It is demonstrated that OpuA is capable of importing the sulfobetaine dimethylsulfonioacetate (DMSA) and important principles that enable OpuAC to specifically bind various compatible solutes were uncovered.
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Functional immobilization of a DNA-binding protein at a membrane interface via histidine tag and synthetic chelator lipids.
TL;DR: The coupling of a DNA-binding protein to self-organized lipid monolayers is examined at the air−water interface by means of film balance techniques and epifluorescence microscopy.
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The GTPase Activity of Murine Guanylate-binding Protein 2 (mGBP2) Controls the Intracellular Localization and Recruitment to the Parasitophorous Vacuole of Toxoplasma gondii
Elisabeth Kravets,Daniel Degrandi,Stefanie Weidtkamp-Peters,Britta Ries,Carolin Konermann,Suren Felekyan,Julia M. Dargazanli,Gerrit J. K. Praefcke,Claus A. M. Seidel,Lutz Schmitt,Sander H. J. Smits,Klaus Pfeffer +11 more
TL;DR: The consistent results indicate that GTP binding, self-assembly, and stimulated hydrolysis activity are required for physiological localization of the protein in infected and uninfected cells and show that the GTPase domain regulates efficient recruitment to T. gondii in response to IFN-γ.
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Double-strand DNA end-binding and sliding of the toroidal CRISPR-associated protein Csn2
Zihni Arslan,Reinhild Wurm,Oleksandr Brener,Philipp Ellinger,Luitgard Nagel-Steger,Filipp Oesterhelt,Lutz Schmitt,Dieter Willbold,Rolf Wagner,Holger Gohlke,Sander H. J. Smits,Ümit Pul +11 more
TL;DR: The results demonstrate that the ring-shaped Csn2 tetramer binds DNA ends through its central hole and slides inward, likely by a screw motion along the helical path of the enclosed DNA.