1JI4

NAP protein from helicobacter pylori

Summary for 1JI4

• Entry DOI: 10.2210/pdb1ji4/pdb
• Related: 1DPS 1QGH
• Descriptor: NEUTROPHIL-ACTIVATING PROTEIN A, FE (III) ION, UNKNOWN ATOM OR ION, ... (5 entities in total)
• Functional Keywords: dodecamer, four-helix bundle, metal transport
• Biological source: Helicobacter pylori
• Cellular location: Cytoplasm: P43313
• Total number of polymer chains: 12
• Total formula weight: 205612.98

Authors

Zanotti, G.,Papinutto, E.,Dundon, W.G.,Battistutta, R.,Seveso, M.,Del Giudice, G.,Rappuoli, R.,Montecucco, C. (deposition date: 2001-06-29, release date: 2002-10-09, Last modification date: 2023-08-16)

Primary citation

Zanotti, G.,Papinutto, E.,Dundon, W.G.,Battistutta, R.,Seveso, M.,Del Giudice, G.,Rappuoli, R.,Montecucco, C.
Structure of the Neutrophil-activating Protein from Helicobacter pylori
J.Mol.Biol., 323:125-130, 2002

PubMed Abstract: Helicobacter pylori is a major human pathogen associated with severe gastroduodenal diseases, including ulcers and cancers. An H.pylori protein that is highly immunogenic in humans and mice has been identified recently. This protein has been termed HP-NAP, due to its ability of activating neutrophils. In order to achieve a molecular understanding of its unique immunogenic and pro-inflammatory properties, we have determined its three-dimensional structure. Its quaternary structure is similar to that of the dodecameric bacterial ferritins (Dps-like family), but it has a different surface potential charge distribution. This is due to the presence of a large number of positively charged residues, which could well account for its unique ability in activating human leukocytes.

PubMed: 12368104
DOI: 10.1016/S0022-2836(02)00879-3

Experimental method

X-RAY DIFFRACTION (2.52 Å)