Publikationen

 

2018

Czech L., Hermann L., Stöveken N., Richter A., Höppner A., Smits S., Heider J., Bremer E. Role of the extremolytes ectoine and hydroxyectoine as both stress protectants and nutrients: genetics, phylogenomics, biochemistry, and structural analysis. Genes. 2018; 22;9(4). pii: E177. doi: 10.3390/genes9040177

Hoffmann T., Warmbold B., Smits S.H., Tschapek B.,Ronzheimer S., Bashir A., Chen C., Rolbetzki A., Pittelkow M., Jebbar M., Seubert A., Schmitt L., Bremer E. (2018) Arsenobetaine: an ecophysiologically important organoarsenical confers cytoprotection against osmotic stress and growth temperature extremes Environmental Microbiology 20(1): 305-323. doi: 10.1111/1462-2920

2017

Zhao C., Höppner A., Xu Q.-Z. , Gärtner W., Scheer H. , Zhou M. , Zhao K.-H. . Structures and enzymatic mechanisms of phycobiliprotein lyases CpcE/F and PecE/F. Proc. Natl. Acad. Sci. U S A. 2017;  114(50):13170-13175. doi: 10.1073/pnas.1715495114

Minges, A., Ciupka, D., Winkler, C., Hoppner, A., Gohlke, H., and Groth, G. (2017a). Structural intermediates and directionality of the swiveling motion of Pyruvate Phosphate Dikinase. Sci Rep 7, 45389. doi: 10.1038/srep45389.

Minges, A., Hoppner, A., and Groth, G. (2017b). Trapped intermediate state of plant pyruvate phosphate dikinase indicates substeps in catalytic swiveling domain mechanism. Protein Sci 26, 1667-1673. doi: 10.1002/pro.3184.

Reiners, J., Abts, A., Clemens, R., Smits, S.H., and Schmitt, L. (2017). Stoichiometry and structure of a lantibiotic maturation complex. Sci Rep 7, 42163. doi: 10.1038/srep42163.

Teichmann, L., Chen, C., Hoffmann, T., Smits, S.H.J., Schmitt, L., and Bremer, E. (2017). From substrate specificity to promiscuity: hybrid ABC transporters for osmoprotectants. Mol Microbiol 104, 761-780. doi: 10.1111/mmi.13660.

2016

Diedrich, D., Moita, A.J., Ruther, A., Frieg, B., Reiss, G.J., Hoeppner, A., Kurz, T., Gohlke, H., Ludeke, S., Kassack, M.U., and Hansen, F.K. (2016). alpha-Aminoxy Oligopeptides: Synthesis, Secondary Structure, and Cytotoxicity of a New Class of Anticancer Foldamers. Chemistry 22, 17600-17611. doi: 10.1002/chem.201602521.

Khosa, S., Frieg, B., Mulnaes, D., Kleinschrodt, D., Hoeppner, A., Gohlke, H., and Smits, S.H. (2016a). Structural basis of lantibiotic recognition by the nisin resistance protein from Streptococcus agalactiae. Sci Rep 6, 18679. doi: 10.1038/srep18679.

Khosa, S., Hoeppner, A., Gohlke, H., Schmitt, L., and Smits, S.H. (2016b). Structure of the Response Regulator NsrR from Streptococcus agalactiae, Which Is Involved in Lantibiotic Resistance. PLoS One 11, e0149903. doi: 10.1371/journal.pone.0149903.

Widderich, N., Kobus, S., Hoppner, A., Riclea, R., Seubert, A., Dickschat, J.S., Heider, J., Smits, S.H., and Bremer, E. (2016). Biochemistry and Crystal Structure of Ectoine Synthase: A Metal-Containing Member of the Cupin Superfamily. PLoS One 11, e0151285. doi: 10.1371/journal.pone.0151285.

2015

Broy, S., Chen, C., Hoffmann, T., Brock, N.L., Nau-Wagner, G., Jebbar, M., Smits, S.H., Dickschat, J.S., and Bremer, E. (2015). Abiotic stress protection by ecologically abundant dimethylsulfoniopropionate and its natural and synthetic derivatives: insights from Bacillus subtilis. Environ Microbiol 17, 2362-2378. doi: 10.1111/1462-2920.12698.

Khosa, S., Hoeppner, A., Kleinschrodt, D., and Smits, S.H. (2015a). Overexpression, purification and crystallization of the response regulator NsrR involved in nisin resistance. Acta Crystallogr F Struct Biol Commun 71, 1322-1326. doi: 10.1107/S2053230X15016441.

Khosa, S., Hoeppner, A., Kleinschrodt, D., and Smits, S.H. (2015b). Overexpression, purification, crystallization and preliminary X-ray diffraction of the nisin resistance protein from Streptococcus agalactiae. Acta Crystallogr F Struct Biol Commun 71, 671-675. doi: 10.1107/S2053230X15006226.

Kobus, S., Widderich, N., Hoeppner, A., Bremer, E., and Smits, S.H. (2015). Overproduction, crystallization and X-ray diffraction data analysis of ectoine synthase from the cold-adapted marine bacterium Sphingopyxis alaskensis. Acta Crystallogr F Struct Biol Commun 71, 1027-1032. doi: 10.1107/S2053230X15011115.

Tang, K., Ding, W.L., Hoppner, A., Zhao, C., Zhang, L., Hontani, Y., Kennis, J.T., Gartner, W., Scheer, H., Zhou, M., and Zhao, K.H. (2015). The terminal phycobilisome emitter, LCM: A light-harvesting pigment with a phytochrome chromophore. Proc Natl Acad Sci U S A 112, 15880-15885. doi: 10.1073/pnas.1519177113.

2014

Bashir, A., Hoffmann, T., Kempf, B., Xie, X., Smits, S.H., and Bremer, E. (2014a). Plant-derived compatible solutes proline betaine and betonicine confer enhanced osmotic and temperature stress tolerance to Bacillus subtilis. Microbiology 160, 2283-2294. doi: 10.1099/mic.0.079665-0.

Bashir, A., Hoffmann, T., Smits, S.H., and Bremer, E. (2014b). Dimethylglycine provides salt and temperature stress protection to Bacillus subtilis. Appl Environ Microbiol 80, 2773-2785. doi: 10.1128/AEM.00078-14.

Gawarzewski, I., DiMaio, F., Winterer, E., Tschapek, B., Smits, S.H., Jose, J., and Schmitt, L. (2014). Crystal structure of the transport unit of the autotransporter adhesin involved in diffuse adherence from Escherichia coli. J Struct Biol 187, 20-29. doi: 10.1016/j.jsb.2014.05.003.

Gunne, M., Hoppner, A., Hagedoorn, P.L., and Urlacher, V.B. (2014). Structural and redox properties of the small laccase Ssl1 from Streptomyces sviceus. FEBS J 281, 4307-4318. doi: 10.1111/febs.12755.

Hoeppner, A., Widderich, N., Bremer, E., and Smits, S.H. (2014). Overexpression, crystallization and preliminary X-ray crystallographic analysis of the ectoine hydroxylase from Sphingopyxis alaskensis. Acta Crystallogr F Struct Biol Commun 70, 493-496. doi: 10.1107/S2053230X14004798.

Hoppner, A., Widderich, N., Lenders, M., Bremer, E., and Smits, S.H. (2014). Crystal structure of the ectoine hydroxylase, a snapshot of the active site. J Biol Chem 289, 29570-29583. doi: 10.1074/jbc.M114.576769.

Schlieper, D., Forster, K., Paulus, J.K., and Groth, G. (2014). Resolving the activation site of positive regulators in plant phosphoenolpyruvate carboxylase. Mol Plant 7, 437-440. doi: 10.1093/mp/sst130.

Widderich, N., Hoppner, A., Pittelkow, M., Heider, J., Smits, S.H., and Bremer, E. (2014a). Biochemical properties of ectoine hydroxylases from extremophiles and their wider taxonomic distribution among microorganisms. PLoS One 9, e93809. doi: 10.1371/journal.pone.0093809.

Widderich, N., Pittelkow, M., Hoppner, A., Mulnaes, D., Buckel, W., Gohlke, H., Smits, S.H., and Bremer, E. (2014b). Molecular dynamics simulations and structure-guided mutagenesis provide insight into the architecture of the catalytic core of the ectoine hydroxylase. J Mol Biol 426, 586-600. doi: 10.1016/j.jmb.2013.10.028.

2013

Gawarzewski, I., Tschapek, B., Hoeppner, A., Jose, J., Smits, S.H., and Schmitt, L. (2013). Purification, crystallization and preliminary X-ray crystallographic analysis of the transport unit of the monomeric autotransporter AIDA-I from Escherichia coli. Acta Crystallogr Sect F Struct Biol Cryst Commun 69, 1159-1162. doi: 10.1107/S1744309113024366.

Gohlke, H., Hergert, U., Meyer, T., Mulnaes, D., Grieshaber, M.K., Smits, S.H., and Schmitt, L. (2013). Binding region of alanopine dehydrogenase predicted by unbiased molecular dynamics simulations of ligand diffusion. J Chem Inf Model 53, 2493-2498. doi: 10.1021/ci400370y.

Hoeppner, A., Schmitt, L., and Smits, S.H. (2013). Proteins and Their Ligands: Their Importance and How to Crystallize Them. InTech Open.

Hoppner, A., Schomburg, D., and Niefind, K. (2013). Enzyme-substrate complexes of the quinate/shikimate dehydrogenase from Corynebacterium glutamicum enable new insights in substrate and cofactor binding, specificity, and discrimination. Biol Chem 394, 1505-1516. doi: 10.1515/hsz-2013-0170.

Paulus, J.K., Schlieper, D., and Groth, G. (2013). Greater efficiency of photosynthetic carbon fixation due to single amino-acid substitution. Nat Commun 4, 1518. doi: 10.1038/ncomms2504.

Vasudevan, A.A., Smits, S.H., Hoppner, A., Haussinger, D., Koenig, B.W., and Munk, C. (2013). Structural features of antiviral DNA cytidine deaminases. Biol Chem 394, 1357-1370. doi: 10.1515/hsz-2013-0165.

2012 

Ellinger, P., Arslan, Z., Wurm, R., Tschapek, B., MacKenzie, C., Pfeffer, K., Panjikar, S., Wagner, R., Schmitt, L., Gohlke, H., Pul, U., and Smits, S.H. (2012). The crystal structure of the CRISPR-associated protein Csn2 from Streptococcus agalactiae. J Struct Biol 178, 350-362. doi: 10.1016/j.jsb.2012.04.006.

Hoeppner, A., Thomas, F., Rueppel, A., Hensel, R., Blankenfeldt, W., Bayer, P., and Faust, A. (2012). Structure of the corrinoid:coenzyme M methyltransferase MtaA from Methanosarcina mazei. Acta Crystallogr D Biol Crystallogr 68, 1549-1557. doi: 10.1107/S090744491203853X.

van Os, N., Smits, S.H., Schmitt, L., and Grieshaber, M.K. (2012). Control of D-octopine formation in scallop adductor muscle as revealed through thermodynamic studies of octopine dehydrogenase. J Exp Biol 215, 1515-1522. doi: 10.1242/jeb.069344.

2011

Abts, A., Schwarz C.K., Tschapek B., Smits S.H., and L., S. (2011). Rational and irrational approaches to convince a protein to crystallize. InTech Open.

Pittelkow, M., Tschapek, B., Smits, S.H., Schmitt, L., and Bremer, E. (2011). The crystal structure of the substrate-binding protein OpuBC from Bacillus subtilis in complex with choline. J Mol Biol 411, 53-67. doi: 10.1016/j.jmb.2011.05.037.

Schwarz, C.K., Tschapek, B., Jumpertz, T., Jenewein, S., Lecher, J., Willbold, D., Panjikar, S., Holland, I.B., Smits, S.H., and Schmitt, L. (2011). 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. Acta Crystallogr Sect F Struct Biol Cryst Commun 67, 630-633. doi: 10.1107/S1744309111010876.

Smits, S.H., Meyer, T., Mueller, A., van Os, N., Stoldt, M., Willbold, D., Schmitt, L., and Grieshaber, M.K. (2010). Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography. PLoS One 5, e12312. doi: 10.1371/journal.pone.0012312.

Tschapek, B., Pittelkow, M., Sohn-Bosser, L., Holtmann, G., Smits, S.H., Gohlke, H., Bremer, E., and Schmitt, L. (2011). Arg149 is involved in switching the low affinity, open state of the binding protein AfProX into its high affinity, closed state. J Mol Biol 411, 36-52. doi: 10.1016/j.jmb.2011.05.039.

 

 

 

 

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