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Insertion of a chaperone domain converts FKBP12 into a powerful catalyst of protein folding

Title data

Knappe, Thomas A. ; Eckert, Barbara ; Schaarschmidt, Peter ; Scholz, Christian ; Schmid, Franz X.:
Insertion of a chaperone domain converts FKBP12 into a powerful catalyst of protein folding.
In: Journal of Molecular Biology. Vol. 368 (18 May 2007) Issue 5 . - pp. 1458-1468.
ISSN 0022-2836

Official URL: Volltext

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Abstract in another language

The catalytic activity of human FKBP12 as a prolyl isomerase is high towards short peptides, but very low in proline-limited protein folding reactions. In contrast, the SlyD proteins, which are members of the FKBP family, are highly active as folding enzymes. They contain an extra "insert-in-flap" or IF domain near the prolyl isomerase active site. The excision of this domain did not affect the prolyl isomerase activity of SlyD from Escherichia coli towards short peptide substrates but abolished its catalytic activity in proline-limited protein folding reactions. The reciprocal insertion of the IF domain of SlyD into human FKBP12 increased its folding activity 200-fold and generated a folding catalyst that is more active than SlyD itself. The IF domain binds to refolding protein chains and thus functions as a chaperone module. A prolyl isomerase catalytic site and a separate chaperone site with an adapted affinity for refolding protein chains are the key elements for a productive coupling between the catalysis of prolyl isomerization and conformational folding in the enzymatic mechanisms of SlyD and other prolyl isomerases, such as trigger factor and FkpA.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 17397867
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Professorship Biochemistry - Univ.-Prof. Dr. Franz Xaver Schmid
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 24 Apr 2015 07:40
Last Modified: 28 May 2015 15:31
URI: https://eref.uni-bayreuth.de/id/eprint/10631