Pal

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Structure

Pal is a lipoprotein which is anchored in the outer membrane with an approximate length of 173 amino acids in the precursor form. It contains a signal sequence including an LVAC motif, with the flexible, hydrophobic N-terminal tail binding to the inner leaflet of the outer membrane and anchoring it. During translocation, signal peptidase II cleaves the LVAC motif, and the localisation of Pal is dependent on the Lol protein system. Serine, the amino acid at #2 position in the mature protein is a localisation determinant for the position of Pal in the outer membrane[1].

Pal forms a complex with TolB (see TolB).

Template:STRUCTURE 1oap

Function

One of the roles of Pal is thought to be an anchor, linking the outer membrane to the peptidoglycan layer and offering support to this connection[2]. It is also possible that Pal is involved in the translocation of subunits of the surface O-antigens, affecting its structure[1].

Pal is also thought to play a significant role in the process of pathogenesis. The protein is highly immunogenic, which also makes them suitable candidates for the production of vaccines[1].

References

  1. ↑ 1.0 1.1 1.2 Godlewska R, Wisniewska K, Pietras Z, Jagusztyn-Krynicka EK. Peptidoglycan-associated lipoprotein (Pal) of Gram-negative bacteria: function, structure, role in pathogenesis and potential application in immunoprophylaxis. FEMS Microbiol Lett. 2009 Sep;298(1):1-11. Epub 2009 May 21. PMID:19519769 doi:10.1111/j.1574-6968.2009.01659.x
  2. ↑ Parsons LM, Orban J. NMR assignment of the periplasmic domain of peptidoglycan-associated lipoprotein (Pal) from Haemophilus influenzae. J Biomol NMR. 2005 May;32(1):93. PMID:16041489 doi:10.1007/s10858-005-3676-x

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Laura McCauley, Joel L. Sussman

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