5I7P

Crystal structure of Fkbp12-IF(SlyD), a chimeric protein of human Fkbp12 and the insert in flap domain of Ecoli SlyD

Summary for 5I7P

• Entry DOI: 10.2210/pdb5i7p/pdb
• Descriptor: Peptidyl-prolyl cis-trans isomerase FKBP1A,FKBP-type peptidyl-prolyl cis-trans isomerase SlyD,Peptidyl-prolyl cis-trans isomerase FKBP1A (2 entities in total)
• Functional Keywords: fkbp12, prolyl isomerization, chaperone, slyd, "insert in flap", chimeric protein, protein design, isomerase
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm: P62942
• Total number of polymer chains: 1
• Total formula weight: 18105.37

Authors

Jakob, R.P.,Knappe, T.A.,Dobbek, H.,Schmid, F.X. (deposition date: 2016-02-18, release date: 2017-03-08, Last modification date: 2026-04-22)

Primary citation

Zoldak, G.,Knappe, T.A.,Geitner, A.J.,Scholz, C.,Dobbek, H.,Schmid, F.X.,Jakob, R.P.
Bacterial Chaperone Domain Insertions Convert Human FKBP12 into an Excellent Protein-Folding Catalyst-A Structural and Functional Analysis.
Molecules, 29:-, 2024

PubMed Abstract: Many folding enzymes use separate domains for the binding of substrate proteins and for the catalysis of slow folding reactions such as prolyl isomerization. FKBP12 is a small prolyl isomerase without a chaperone domain. Its folding activity is low, but it could be increased by inserting the chaperone domain from the homolog SlyD of near the prolyl isomerase active site. We inserted two other chaperone domains into human FKBP12: the chaperone domain of SlpA from , and the chaperone domain of SlyD from sp. Both stabilized FKBP12 and greatly increased its folding activity. The insertion of these chaperone domains had no influence on the FKBP12 and the chaperone domain structure, as revealed by two crystal structures of the chimeric proteins. The relative domain orientations differ in the two crystal structures, presumably representing snapshots of a more open and a more closed conformation. Together with crystal structures from SlyD-like proteins, they suggest a path for how substrate proteins might be transferred from the chaperone domain to the prolyl isomerase domain.

PubMed: 38611720
DOI: 10.3390/molecules29071440

Experimental method

X-RAY DIFFRACTION (2.002 Å)