2PYB

Napa protein from borrelia burgdorferi

Summary for 2PYB

• Entry DOI: 10.2210/pdb2pyb/pdb
• Related: 1DPS 1JI4 1JI5 1JIG
• Descriptor: Neutrophil activating protein, FE (III) ION (3 entities in total)
• Functional Keywords: ferritin, dps, four-helix bundle, metal transport
• Biological source: Borrelia burgdorferi
• Total number of polymer chains: 4
• Total formula weight: 71544.75

Authors

Zanotti, G.,Papinutto, E.,De Bernard, M. (deposition date: 2007-05-16, release date: 2008-08-12, Last modification date: 2024-02-21)

Primary citation

Codolo, G.,Papinutto, E.,Polenghi, A.,D'Elios, M.M.,Zanotti, G.,de Bernard, M.
Structure and immunomodulatory property relationship in NapA of Borrelia burgdorferi.
Biochim.Biophys.Acta, 1804:2191-2197, 2010

PubMed Abstract: NapA from Borrelia burgdorferi is a member of the Dps-like protein family with specific immunomodulatory properties; in particular, NapA is able to induce the expression of IL-23 in neutrophils and monocytes, as well as the expression of IL-6, IL-1β, and transforming growth factor beta (TGF-β) in monocytes, via Toll-like receptor (TLR) 2. Such an activity on innate immune cells triggers a synovial fluid Th17 response. Here we report the crystal structure of NapA, determined at 2.6Å resolution, which shows that the quaternary structure of the protein is that of a dodecamer with 23 symmetry, typical of the proteins of the family. We also demonstrate that the N- and C-terminal tails, which are flexible and not visible in the crystal, are not relevant for its pro-Th17 activity. Based on the crystal structure and on the comparison with the structure of the orthologous protein from Helicobacter pylori, HP-NAP, we hypothesize that the charge distributions on the two proteins' surfaces are responsible for the interaction with TLR2 and for the different behaviors in modulating the immune response.

PubMed: 20851780
DOI: 10.1016/j.bbapap.2010.09.004

Experimental method

X-RAY DIFFRACTION (2.6 Å)