PDBsum entry 1ix5

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Isomerase PDB id
Protein chain
151 a.a. *
* Residue conservation analysis

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Key reference
Title Three-Dimensional solution structure of an archaeal fkbp with a dual function of peptidyl prolyl cis-Trans isomerase and chaperone-Like activities.
Authors R.Suzuki, K.Nagata, F.Yumoto, M.Kawakami, N.Nemoto, M.Furutani, K.Adachi, T.Maruyama, M.Tanokura.
Ref. J Mol Biol, 2003, 328, 1149-1160. [DOI no: 10.1016/S0022-2836(03)00379-6]
PubMed id 12729748
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.
Figure 4.
Figure 4. Overlay of the solution structure of MtFKBP17 and the crystal structure of HsFKBP12. The C^a atoms used for superimposition are colored red and blue, while the other C^a atoms are colored pink and light blue in MtFKBP17 and HsFKBP12, respectively.
Figure 8.
Figure 8. Hydrophobic surface of the IF domain of MtFKBP17. Amino acid residues forming the hydrophobic surface are shown and labeled.
The above figures are reprinted by permission from Elsevier: J Mol Biol (2003, 328, 1149-1160) copyright 2003.
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