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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New examples of membrane protein expression and purification using the yeast based Pdr1-3 expression strategy
TL;DR: The application of this yeast based expression system that is suitable for cloning, expression and purification of a wide variety of membrane proteins is demonstrated.
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Crystallization and preliminary X-ray crystallographic studies of an oligomeric species of a refolded C39 peptidase-like domain of the Escherichia coli ABC transporter haemolysin B.
Christian Schwarz,Britta Tschapek,Thorsten Jumpertz,Stefan Jenewein,Justin Lecher,Justin Lecher,Dieter Willbold,Dieter Willbold,Santosh Panjikar,I. Barry Holland,Sander H. J. Smits,Lutz Schmitt +11 more
TL;DR: The overexpression, purification and crystallization of the isolated C39-like domain are described as a first step towards obtaining structural insights into this domain and eventually answering the question concerning the function of a degenerated C39 domain in the ABC transporter HlyB.
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Transmitting the energy: interdomain cross-talk in Pdr5.
TL;DR: Current knowledge of the interdomain cross-talk as well as new results obtained for asymmetric ABC transporters are summarized and discussed and possible structural and functional implications for Pdr5 are derived.
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Identity Determinants of the Translocation Signal for a Type 1 Secretion System
Olivia Spitz,I Erenburg,Kerstin Kanonenberg,Sandra Peherstorfer,Michael H. H. Lenders,Jens Reiners,Miao Ma,Ben F. Luisi,Sander H. J. Smits,Lutz Schmitt +9 more
TL;DR: Combined structure prediction based on the AlphaFold algorithm together with functional and in silico data to examine the role of secondary structure in secretion propose a C-terminal, amphipathic helix that plays an essential role in the early steps of the secretion process.
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The periplasmic chaperone Skp prevents misfolding of the secretory lipase A from Pseudomonas aeruginosa
Athanasios Papadopoulos,Max Busch,Jens Reiners,Eymen Hachani,Miriam Bäumers,Lutz Schmitt,Karl-Erich Jaeger,Filip Kovacic,Sander H. J. Smits,Alexej Kedrov +9 more
TL;DR: In this article , the periplasmic chaperone Skp of Pseudomonas aeruginosa, but not SurA, FkpA, PpiD or YfgM, efficiently prevents misfolding of the aggregation-prone lipase A and facilitates its activation by a specific foldase LipH.