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Stefan Jenewein
Researcher at University of Düsseldorf
Publications - 10
Citations - 804
Stefan Jenewein is an academic researcher from University of Düsseldorf. The author has contributed to research in topics: ATP-binding cassette transporter & Central element. The author has an hindex of 7, co-authored 10 publications receiving 775 citations. Previous affiliations of Stefan Jenewein include Goethe University Frankfurt.
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Journal ArticleDOI
H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB
TL;DR: The hypothesis that substrate‐assisted catalysis, rather than general base catalysis might operate in ABC‐ATPases is discussed, based on biochemical experiments, and proposed model in which E631 and H662, highly conserved among ABC transporters, form a catalytic dyad.
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A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer.
Jelena Zaitseva,Christine Oswald,Thorsten Jumpertz,Stefan Jenewein,Alexander Wiedenmann,I. Barry Holland,Lutz Schmitt +6 more
TL;DR: The basic set of crystal structures necessary to describe the catalytic cycle of the isolated HlyB‐NBD (nucleotide‐binding domain) has now been completed, allowing a detailed analysis with respect to hinge regions, functionally important key residues and potential energy storage devices that revealed many novel features.
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Functional characterization and ATP-induced dimerization of the isolated ABC-domain of the haemolysin B transporter.
Jelena Zaitseva,Stefan Jenewein,Alexander Wiedenmann,Houssain Benabdelhak,I. Barry Holland,Lutz Schmitt +5 more
TL;DR: Experimental data showed that both the nature and pH of an assay buffer influenced the level of protein activity, and comparative analysis of protein stability and ATPase activity in various buffers suggests an inverse relationship between the two.
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The rate of folding dictates substrate secretion by the Escherichia coli hemolysin type 1 secretion system.
TL;DR: The efficiency of secretion by the Hly system is dictated by the folding rate of the substrate, and it is demonstrated that fusion proteins defective in export can be engineered for secretion while still retaining function.
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Molecular insights into the mechanism of ATP-hydrolysis by the NBD of the ABC-transporter HlyB.
TL;DR: It is suggested that substrate‐assisted catalysis (SAC), but not general base catalysis, is responsible for ATP‐hydrolysis in this NBD and might also operate in other NBDs.