PDBsum entry 2pyb

Metal transport

PDB id: 2pyb

Contents

Protein chains

151 a.a. *

Metals

_FE ×8

Waters ×24

* Residue conservation analysis

PDB id:

2pyb

Name:

Metal transport

Title:

Napa protein from borrelia burgdorferi

Structure:

Neutrophil activating protein. Chain: a, b, c, d. Synonym: napa. Engineered: yes

Source:

Borrelia burgdorferi. Strain: b31. Gene: napa. Expressed in: bacillus subtilis. Expression_system_taxid: 1423.

Resolution:

2.60Å R-factor: 0.242 R-free: 0.275

Authors:

G.Zanotti,E.Papinutto,M.De Bernard

Key ref:

G.Codolo et al. (2010). Structure and immunomodulatory property relationship in NapA of Borrelia burgdorferi. Biochim Biophys Acta, 1804, 2191-2197. PubMed id: 20851780

Date:

16-May-07 Release date: 12-Aug-08

Protein chains

O51633  (O51633_BORBU) -  Neutrophil activating protein A (NapA) from Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)

Seq: 178 a.a.

Struc: 151 a.a.

Enzyme reactions

• Enzyme class: E.C.?

Biochim Biophys Acta 1804:2191-2197 (2010)

PubMed id: 20851780

Structure and immunomodulatory property relationship in NapA of Borrelia burgdorferi.

G.Codolo, E.Papinutto, A.Polenghi, M.M.D'Elios, G.Zanotti, M.de Bernard.

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.