Binding analysis of a psychrotrophic FKBP22 to a folding intermediate of protein using surface plasmon resonance.
SIB1 FKBP22 is a homodimer, with each subunit consisting of the C-terminal catalytic domain and N-terminal dimerization domain. This protein exhibits peptidyl prolyl cis-trans isomerase activity for both peptide and protein substrates. However, truncation of the N-terminal domain greatly reduces the activity only for a protein substrate. Using surface plasmon resonance, we showed that SIB1 FKBP22 loses the binding ability to a folding intermediate of protein upon truncation of the N-terminal domain but does not lose it upon truncation of the C-terminal domain. We propose that the binding site of SIB1 FKBP22 to a protein substrate of PPIase is located at the N-terminal domain.
Suzuki
Yutaka
Y
Department of Material and Life Science, Graduate School of Engineering, Osaka University, Japan.
Win
Ohnmar Ye
OY
Koga
Yuichi
Y
Takano
Kazufumi
K
Kanaya
Shigenori
S
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D007768:Lactalbumin / Q000737:chemistry; D010084:Oxidation-Reduction; D019696:Peptidylprolyl Isomerase / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D020592:Shewanella / Q000378:metabolism*; D020349:Surface Plasmon Resonance; D022021:Tacrolimus Binding Proteins / Q000737:chemistry* / Q000378:metabolism
D001426:Bacterial Proteins; D007768:Lactalbumin; C403422:FKBP22; D022021:Tacrolimus Binding Proteins; D019696:Peptidylprolyl Isomerase