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Results: 4
Crystal structures of the precursor form of glucose-fructose oxidoreductase from Zymomonas mobilis and its complexes with bound ligands
Authors: Nurizzo, D Halbig, D Sprenger, GA Baker, EN
Citation: D. Nurizzo et al., Crystal structures of the precursor form of glucose-fructose oxidoreductase from Zymomonas mobilis and its complexes with bound ligands, BIOCHEM, 40(46), 2001, pp. 13857-13867
Crystal structure of a truncated mutant of glucose-fructose oxidoreductaseshows that an N-terminal arm controls tetramer formation
Authors: Lott, JS Halbig, D Baker, HM Hardman, MJ Sprenger, GA Baker, EN
Citation: Js. Lott et al., Crystal structure of a truncated mutant of glucose-fructose oxidoreductaseshows that an N-terminal arm controls tetramer formation, J MOL BIOL, 304(4), 2000, pp. 575-584
Bacterial proteins carrying twin-R signal peptides are specifically targeted by the Delta pH-dependent transport machinery of the thylakoid membrane system
Authors: Halbig, D Hou, B Freudl, R Sprenger, GA Klosgen, RB
Citation: D. Halbig et al., Bacterial proteins carrying twin-R signal peptides are specifically targeted by the Delta pH-dependent transport machinery of the thylakoid membrane system, FEBS LETTER, 447(1), 1999, pp. 95-98
The efficient export of NADP-containing glucose-fructose oxidoreductase tothe periplasm of Zymomonas mobilis depends both on an intact twin-argininemotif in the signal peptide and on the generation of a structural export signal induced by cofactor binding
Authors: Halbig, D Wiegert, T Blaudeck, N Freudl, R Sprenger, GA
Citation: D. Halbig et al., The efficient export of NADP-containing glucose-fructose oxidoreductase tothe periplasm of Zymomonas mobilis depends both on an intact twin-argininemotif in the signal peptide and on the generation of a structural export signal induced by cofactor binding, EUR J BIOCH, 263(2), 1999, pp. 543-551
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