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TitleBacterial Chaperone Domain Insertions Convert Human FKBP12 into an Excellent Protein-Folding Catalyst-A Structural and Functional Analysis.
Journal, issue, pagesMolecules, Vol. 29, Year 2024
Publish dateFeb 18, 2016 (structure data deposition date)
AuthorsZoldak, G. / Knappe, T.A. / Geitner, A.J. / Scholz, C. / Dobbek, H. / Schmid, F.X. / Jakob, R.P.
External linksMolecules / PubMed:38611720
MethodsX-ray diffraction
Resolution1.9 - 2.002 Å
Structure data

PDB-5i7p:
Crystal structure of Fkbp12-IF(SlyD), a chimeric protein of human Fkbp12 and the insert in flap domain of Ecoli SlyD
Method: X-RAY DIFFRACTION / Resolution: 2.002 Å

PDB-5i7q:
Crystal structure of Fkbp12-IF(SlpA), a chimeric protein of human Fkbp12 and the insert in flap domain of Ecoli SlpA
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • escherichia coli (E. coli)
KeywordsISOMERASE / Fkbp12 / prolyl isomerization / chaperone / SlyD / "insert in flap" / chimeric protein / protein design / SlpA / PPIase

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