title: NMR assignments of the peptidyl-prolyl cis-trans isomerase domain of trigger factor from E. coli.
abstract: Trigger factor (TF) is a highly conserved multi-domain molecular chaperone in bacteria. It binds via its ribosome binding domain (RBD) to the ribosomal tunnel exit and facilitates co-translational folding of a broad range of protein substrates primarily through interactions with the substrate binding domain (SBD) adjacent to the RBD. Within the SBD, a peptidyl-prolyl cis-trans isomerase (PPIase) domain is inserted leading to an unusual domain insertion, which may provide stabilizing effect to the highly plastic SBD. Here we report the near complete NMR assignments of TF PPIase providing the basis for subsequent structural and folding in the context of the chaperone activity of TF.
authors.affiliation: Institute of Biological Chemistry, Academia Sinica, Taipei, 11529, Taiwan.|Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 30013, Taiwan.
authors.forename: Chih-Ting
authors.initials: CT
authors.lastname: Huang
authors.affiliation: Institute of Biological Chemistry, Academia Sinica, Taipei, 11529, Taiwan. sthsu@gate.sinica.edu.tw.|Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 30013, Taiwan. sthsu@gate.sinica.edu.tw.|Institute of Biochemical Sciences, National Taiwan University, Taipei, 10617, Taiwan. sthsu@gate.sinica.edu.tw.
authors.forename: Shang-Te Danny
authors.initials: ST
authors.lastname: Hsu
mesh_terms: D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D019696:Peptidylprolyl Isomerase / Q000737:chemistry* / Q000378:metabolism; D000072417:Protein Domains; D012270:Ribosomes / Q000378:metabolism
chemical_list: D029968:Escherichia coli Proteins; C403324:trigger factor, E coli; D019696:Peptidylprolyl Isomerase
keywords: Co-translational folding; Molecular chaperone; Peptidyl-prolyl cist-trans isomerase; Trigger factor