at Google ScholarTitle 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
(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 > Professor 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: | 28 Feb 2023 14:00 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/10464 |