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Proteolytic mechanism of a novel mitochondrial and chloroplastic PreP peptidasome.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. (E. Glaser)
(T. Eneqvist)
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. (T. Eneqvist)
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. (E. Glaser)
2006 (English)In: Biol Chem, ISSN 1431-6730, Vol. 387, no 8, 1087-90 p.Article in journal (Refereed) Published
Abstract [en]

The 2.1-A-resolution crystal structure of the novel mitochondrial and chloroplastic metalloendopeptidase, AtPreP1, revealed a unique peptidasome structure, in which the two halves of the enzyme completely enfold a huge proteolytic cavity. Based on the structure, we proposed a novel mechanism for proteolysis involving hinge-bending motions, which cause the protease to open and close in response to substrate binding. We generated four double-mutants of AtPreP1 by introducing cysteines at positions where disulfide bonds can be formed in order to lock and unlock the protease and tested the activity under oxidizing and reducing conditions. The overall results support the proposed mechanism.

Place, publisher, year, edition, pages
2006. Vol. 387, no 8, 1087-90 p.
Keyword [en]
Arabidopsis Proteins/*chemistry, Chloroplasts/*chemistry, Crystallography; X-Ray, Mitochondria/*chemistry, Models; Molecular, Peptide Hydrolases/*chemistry, Protein Conformation, Protein Structure; Tertiary
Identifiers
URN: urn:nbn:se:su:diva-22515PubMedID: 16895479OAI: oai:DiVA.org:su-22515DiVA: diva2:189042
Available from: 2007-12-21 Created: 2007-12-21 Last updated: 2011-01-11Bibliographically approved

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