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Showing papers by "Lutz Schmitt published in 2009"


Journal ArticleDOI
TL;DR: The first case of a child with PFIC‐2 suffering from repeated posttransplant recurrence of progressive intrahepatic cholestasis due to autoantibodies against BSEP is reported, illustrating a novel disease mechanism due to a new class of functionally relevant autoantIBodies resulting in cholESTasis and subsequent liver failure.

118 citations


Journal ArticleDOI
TL;DR: A comparison of the recently described structure of TeaA from Halomonas elongata and an ectoine-binding protein (EhuB) from an ABC transporter revealed a conserved ligand binding mode that involves both directed and cation-pi interactions.

45 citations


Journal ArticleDOI
TL;DR: The crystal structure of ChoX is reported in an unusual, ligand-free conformation that represents a semi-closed form of ChoZ, and comparison with the two well-characterized substrate binding proteins, MBP and HisJ, suggests the presence of a similar subdomain in these proteins.
Abstract: The periplasmic ligand-binding protein ChoX is part of the ABC transport system ChoVWX that imports choline as a nutrient into the soil bacterium Sinorhizobium meliloti. We have recently reported the crystal structures of ChoX in complex with its ligands choline and acetylcholine and the structure of a fully closed but substrate-free state of ChoX. This latter structure revealed an architecture of the ligand-binding site that is superimposable to the closed, ligand-bound form of ChoX. We report here the crystal structure of ChoX in an unusual, ligand-free conformation that represents a semi-closed form of ChoX. The analysis revealed a subdomain movement in the N-lobe of ChoX. Comparison with the two well-characterized substrate binding proteins, MBP and HisJ, suggests the presence of a similar subdomain in these proteins.

22 citations


Journal ArticleDOI
TL;DR: The Membranproteine is ein faszinierendes Forschungsobjekt, fur viele aber auch der schlimmste Alptraum, dem sie je begegnet sind as mentioned in this paper.
Abstract: Fur viele Wissenschaftler sind Membranproteine ein faszinierendes Forschungsobjekt, fur viele aber auch der schlimmste Alptraum, dem sie je begegnet sind. Letztere kampfen mit intrinsischen Problemen: Expression, Reinigung, Stabilitat, biochemische und biophysikalische Charakterisierung; die anderen begeistert die Funktion von Membranproteinen — Informationsaustausch uber biologische Membranen, ohne die wahrscheinlich das Leben, wie wir es heute kennen, nicht existieren wurde.