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Dimeric Structure of the Bacterial Extracellular Foldase PrsA

Title data

Jakob, Roman P. ; Koch, Johanna R. ; Burmann, Björn M. ; Schmidpeter, Philipp A. M. ; Hunkeler, Moritz ; Hiller, Sebastian ; Schmid, Franz X. ; Maier, Timm:
Dimeric Structure of the Bacterial Extracellular Foldase PrsA.
In: The Journal of Biological Chemistry. Vol. 290 (6 February 2015) Issue 6 . - pp. 3278-3292.
ISSN 1083-351X
DOI: https://doi.org/10.1074/jbc.M114.622910

Abstract in another language

Secretion of proteins into the membrane-cell wall space is essential for cell wall biosynthesis and pathogenicity in Gram-positive bacteria. Folding and maturation of many secreted proteins depend on a single extracellular foldase, the PrsA protein. PrsA is a 30-kDa protein, lipid anchored to the outer leaflet of the cell membrane. The crystal structure of Bacillus subtilis PrsA reveals a central catalytic parvulin-type prolyl isomerase domain, which is inserted into a larger composite NC domain formed by the N- and C-terminal regions. This domain architecture resembles, despite a lack of sequence conservation, both trigger factor, a ribosome-binding bacterial chaperone, and SurA, a periplasmic chaperone in Gram-negative bacteria. Two main structural differences are observed in that the N-terminal arm of PrsA is substantially shortened relative to the trigger factor and SurA and in that PrsA is found to dimerize in a unique fashion via its NC domain. Dimerization leads to a large, bowl-shaped crevice, which might be involved in vivo in protecting substrate proteins from aggregation. NMR experiments reveal a direct, dynamic interaction of both the parvulin and the NC domain with secretion propeptides, which have been implicated in substrate targeting to PrsA.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 18164725
Institutions of the University: 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 > Former Professors > Professorship Biochemistry - Univ.-Prof. Dr. Franz Xaver Schmid
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: 21 Apr 2015 13:04
Last Modified: 22 Apr 2015 07:08
URI: https://eref.uni-bayreuth.de/id/eprint/10464