4WO7

Crystal Structure of PrsA from Bacillus subtilis

Summary for 4WO7

• Entry DOI: 10.2210/pdb4wo7/pdb
• Descriptor: Foldase protein PrsA (2 entities in total)
• Functional Keywords: foldase, prolyl isomerase, protein secretion, gram-positive, isomerase
• Biological source: Bacillus subtilis
• Cellular location: Cell membrane ; Lipid-anchor : P24327
• Total number of polymer chains: 2
• Total formula weight: 59954.36

Authors

Jakob, R.P.,Maier, T. (deposition date: 2014-10-15, release date: 2014-12-24, Last modification date: 2024-11-20)

Primary citation

Jakob, R.P.,Koch, J.R.,Burmann, B.M.,Schmidpeter, P.A.,Hunkeler, M.,Hiller, S.,Schmid, F.X.,Maier, T.
Dimeric Structure of the Bacterial Extracellular Foldase PrsA.
J.Biol.Chem., 290:3278-3292, 2015

PubMed Abstract: 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.

PubMed: 25525259
DOI: 10.1074/jbc.M114.622910

Experimental method

X-RAY DIFFRACTION (2.63 Å)