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Dimeric Structure of the Bacterial Extracellular Foldase PrsA.

Artikel i vetenskaplig tidskrift
Författare Roman P Jakob
Johanna R Koch
Björn Marcus Burmann
Philipp A M Schmidpeter
Moritz Hunkeler
Sebastian Hiller
Franz X Schmid
Timm Maier
Publicerad i The Journal of biological chemistry
Volym 290
Nummer/häfte 6
Sidor 3278-92
ISSN 1083-351X
Publiceringsår 2015
Publicerad vid
Sidor 3278-92
Språk en
Länkar dx.doi.org/10.1074/jbc.M114.622910
www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord Amino Acid Sequence, Bacillus subtilis, enzymology, Bacterial Proteins, chemistry, metabolism, Catalytic Domain, Lipoproteins, chemistry, metabolism, Membrane Proteins, chemistry, metabolism, Molecular Sequence Data, Protein Binding, Protein Multimerization
Ämneskategorier Strukturbiologi

Sammanfattning

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.

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