Three-dimensional Solution Structure of an Archaeal FKBP with a Dual Function of Peptidyl Prolyl cis– trans Isomerase and Chaperone-like Activities

• Published in: Journal of molecular biology Vol. 328; no. 5; pp. 1149 - 1160
• Main Authors: Suzuki, Rintaro, Nagata, Koji, Yumoto, Fumiaki, Kawakami, Masaru, Nemoto, Nobuaki, Furutani, Masahiro, Adachi, Kyoko, Maruyama, Tadashi, Tanokura, Masaru
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 16-05-2003
• Subjects: Amino Acid Sequence; archaea; Archaeal Proteins - chemistry; Archaeal Proteins - genetics; Archaeal Proteins - metabolism; Binding Sites; chaperone; FKBP; Methanococcus - genetics; Methanococcus - metabolism; Models, Molecular; Molecular Chaperones - chemistry; Molecular Chaperones - genetics; Molecular Chaperones - metabolism; Molecular Sequence Data; NMR structure determination; Nuclear Magnetic Resonance, Biomolecular; peptidyl-prolyl cis– trans isomerase; Peptidylprolyl Isomerase - chemistry; Peptidylprolyl Isomerase - genetics; Peptidylprolyl Isomerase - metabolism; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Solutions; Static Electricity; Tacrolimus Binding Proteins - chemistry; Tacrolimus Binding Proteins - genetics; Tacrolimus Binding Proteins - metabolism; IF domain, insert in the flap domain; Sly, sensitivity to lysis; archaea; chaperone; HsPvn14, Homo sapiens parvulin-type PPIase (14 kDa; also called hPar14); peptidyl-prolyl cis– trans isomerase; SD, standard deviation; RMSD, root-mean-square deviation; HsFKBP12, Homo sapiens (human) FKBP (12 kDa); Tig, trigger factor; HsFKBP25, Homo sapiens FKBP (25 kDa); OcFKBP52, Oryctolagus cuniculus (rabbit) FKBP (52 kDa); Mip, macrophage infectivity potentiator; RMS, root-mean-square; MtFKBP17, Methanococcus thermolithotrophicus FKBP (17 kDa); Pvn, parvulin; ScFKBP12, Saccharomyces cerevisiae (yeast) FKBP (12 kDa); FKBP, FK506-binding protein; LpFKBP25, Legionella pneumophila FKBP (25 kDa); NOESY, nuclear Overhauser effect spectroscopy; NOE, nuclear Overhauser effect; PPIase, peptidyl prolyl cis– trans isomerase; NMR structure determination; FKBP; HsPvn18, Homo sapiens parvulin-type PPIase with a WW domain (18 kDa; also called hPin1); MgTig51, Mycoplasma genitalium trigger factor (51 kDa); EcTig48, Escherichia coli trigger factor (48 kDa)
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1016/S0022-2836(03)00379-6

Here we report the solution structure of an archaeal FK506-binding protein (FKBP) from a thermophilic archaeum,
Methanococcus thermolithotrophicus (MtFKBP17), which has peptidyl prolyl
cis–
trans isomerase (PPIase) and chaperone-like activities, to reveal the structural basis for the dual function. In addition to a typical PPIase domain, a newly identified domain is formed in the flap loop by a 48-residue insert that is required for the chaperone-like activity. The new domain, called IF domain (the Insert in the Flap), is a novel-folding motif and exposes a hydrophobic surface, which we consider to play an important role in the chaperone-like activity.