title: Chemical shift assignments of the catalytic domain from the yeast proline isomerase Fpr4p.
abstract: Yeast Fpr4p belongs to the FK506-binding protein (FKBP) class of peptidyl proline isomerases (PPIases), and has been implicated in regulating the cis-trans conversion of proline residues within histone tails. Here we report the (1)H, (13)C and (15)N chemical shift assignments for the bacterially expressed C-terminal PPIase catalytic domain of Fpr4p. Prediction of secondary structure reveals similarity to domains from other members of the FKBP proline isomerases, including yeast Fpr1p and the prototypic PPIase region from human FKBP12.
authors: Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, 33607 Pessac Cedex, France.
authors: Yoan R
authors: YR
authors: Monneau
authors: Christopher J
authors: CJ
authors: Nelson
authors: Cameron D
authors: CD
authors: Mackereth
mesh_terms: D000595:Amino Acid Sequence; D020134:Catalytic Domain; D056488:Histone Chaperones / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D019696:Peptidylprolyl Isomerase / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D022021:Tacrolimus Binding Proteins / Q000737:chemistry*
chemical_list: D056488:Histone Chaperones; D029701:Saccharomyces cerevisiae Proteins; D022021:Tacrolimus Binding Proteins; C513494:Fpr4 protein, S cerevisiae; D019696:Peptidylprolyl Isomerase