Author pages are created from data sourced from our academic publisher partnerships and public sources.
Share This Author
A structural classification of substrate‐binding proteins
- R. Berntsson, S. Smits, L. Schmitt, D. Slotboom, B. Poolman
- Biology, MedicineFEBS letters
- 18 June 2010
This work proposes a new classification into six clusters of substrate‐binding proteins, based on features of their three‐dimensional structure, and divides these proteins into three structural classes and two functional classes.
Crystal Structures of the Choline/Acetylcholine Substrate-binding Protein ChoX from Sinorhizobium meliloti in the Liganded and Unliganded-Closed States*
- C. Oswald, S. Smits, +5 authors E. Bremer
- Biology, MedicineJournal of Biological Chemistry
- 21 November 2008
Fluorescence-based ligand binding assays used to quantitate substrate binding by the periplasmic ligand-binding protein ChoX confirmed that ChoX recognizes choline and acetylcholine with high and medium affinity, respectively, and solved the crystal structures of ChoX in a closed, substrate-free conformation.
Crystal structure of the Lrp‐like transcriptional regulator from the archaeon Pyrococcus furiosus
The LrpA structure suggests how the protein might bind and possibly distort its DNA substrate through use of its HtH motifs and control gene expression.
The crystal structure of the substrate-binding protein OpuBC from Bacillus subtilis in complex with choline.
- M. Pittelkow, Britta Tschapek, S. Smits, L. Schmitt, E. Bremer
- Chemistry, MedicineJournal of molecular biology
- 5 August 2011
The crystal structure of theOpuBC/choline complex provides a rational for the observed choline specificity of the OpuB ABC importer in vivo and explains its inability to catalyze the import of glycine betaine into osmotically stressed B. subtilis cells.
NSR from Streptococcus agalactiae confers resistance against nisin and is encoded by a conserved nsr operon
It is shown that NSR from Streptococcus agalactiae (SaNSR) confers 20-fold resistance when expressed in L. lactis and that SaNSR is encoded by an operon structure comprising of a lipoprotein and an ATP-binding cassette transporter as well as a two-component system that is putatively involved in expression and regulation.
Biochemical Properties of Ectoine Hydroxylases from Extremophiles and Their Wider Taxonomic Distribution among Microorganisms
- Nils Widderich, A. Höppner, M. Pittelkow, J. Heider, S. Smits, E. Bremer
- Biology, MedicinePloS one
- 8 April 2014
The genome context of the ect genes was explored to identify proteins that are functionally associated with the synthesis of ectoines; the specialized aspartokinase Ask_Ect and the regulatory protein EctR and this comprehensive in silico analysis was coupled with the biochemical characterization of ectoine hydroxylases.
Lantibiotic Immunity: Inhibition of Nisin Mediated Pore Formation by NisI
- Z. Alkhatib, Marcel Lagedroste, I. Fey, Diana Kleinschrodt, André Abts, S. Smits
- Chemistry, MedicinePloS one
- 11 July 2014
The expression of NisI in combination with externally added nisin mediates an elongation of the chain length of the Lactococcus lactis cocci, and shed light on the immunity of lantibiotic producer strains, and their survival in high levels of their own lentibiotic in the habitat.
Substrate Specificity of the Secreted Nisin Leader Peptidase NisP.
The biochemical characterization of secreted and purified NisP (NisPs) with its natural substrate, the fully modified NisA (mNisA), is presented and the kinetic parameters of NisPs in the presence of NISA containing different modification states are determined.
Role of the Extremolytes Ectoine and Hydroxyectoine as Stress Protectants and Nutrients: Genetics, Phylogenomics, Biochemistry, and Structural Analysis
The biochemistry, phylogenomics, and genetic regulation for the alternative use of ectoines as nutrients are addressed, and an extensive phylogenomic analysis of the ectoine/hydroxyectoine biosynthetic genes is presented.
pH‐induced structural change in a sodium/proton antiporter from Methanococcus jannaschii
The map of MjNhaP1 shows elongated densities in the centre of the dimer and a cluster of density peaks on either side of theDimer core, indicative of a bundle of 4–6 membrane‐spanning helices, which most likely represent the closed and open states of the antiporter.