Structural highlights
Function
[PRSA_BACSU] Essential protein that plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins. Has PPIase activity but it is not essential for its function in vivo.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
PrsA is a peptidyl-prolyl isomerase (PPIase) from Bacillus subtilis belonging to the parvulin family of PPIases. It is a membrane bound lipoprotein at the membrane-wall interface, involved in folding of exported proteins. We present the NMR solution structure of the PPIase domain of PrsA, the first from a Gram-positive bacterium. In addition we mapped out the active site with NMR titration experiments. A high degree of conservation with other members of the parvulin family was revealed in the structure and binding site. Interactions with substrate peptides were also characterized by mutated domains revealing that H122 is indispensable for overall correct folding.
NMR solution structure and characterization of substrate binding site of the PPIase domain of PrsA protein from Bacillus subtilis.,Tossavainen H, Permi P, Purhonen SL, Sarvas M, Kilpelainen I, Seppala R FEBS Lett. 2006 Mar 20;580(7):1822-6. Epub 2006 Feb 24. PMID:16516208[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wahlstrom E, Vitikainen M, Kontinen VP, Sarvas M. The extracytoplasmic folding factor PrsA is required for protein secretion only in the presence of the cell wall in Bacillus subtilis. Microbiology. 2003 Mar;149(Pt 3):569-77. PMID:12634326
- ↑ Tossavainen H, Permi P, Purhonen SL, Sarvas M, Kilpelainen I, Seppala R. NMR solution structure and characterization of substrate binding site of the PPIase domain of PrsA protein from Bacillus subtilis. FEBS Lett. 2006 Mar 20;580(7):1822-6. Epub 2006 Feb 24. PMID:16516208 doi:10.1016/j.febslet.2006.02.042
