3GIO

Crystal structure of the TNF-alpha inducing protein (Tip alpha) from Helicobacter pylori

Summary for 3GIO

• Entry DOI: 10.2210/pdb3gio/pdb
• Descriptor: Putative uncharacterized protein (2 entities in total)
• Functional Keywords: antiparallel beta sheet, four-helix bundle, loop, dna binding protein
• Biological source: Helicobacter pylori
• Total number of polymer chains: 2
• Total formula weight: 42905.36

Authors

Jang, J.Y.,Yoon, H.J.,Yoon, J.Y.,Kim, H.S.,Lee, S.J.,Kim, K.H.,Kim, D.J.,Han, B.G.,Lee, B.I.,Jang, S.,Suh, S.W. (deposition date: 2009-03-05, release date: 2009-08-04, Last modification date: 2024-11-20)

Primary citation

Jang, J.Y.,Yoon, H.J.,Yoon, J.Y.,Kim, H.S.,Lee, S.J.,Kim, K.H.,Kim, D.J.,Jang, S.,Han, B.G.,Lee, B.I.,Suh, S.W.
Crystal Structure of the TNF-alpha-Inducing Protein (Tipalpha) from Helicobacter pylori: Insights into Its DNA-Binding Activity.
J.Mol.Biol., 2009

PubMed Abstract: Helicobacter pylori infection is one of the highest risk factors for gastroduodenal diseases including gastric cancer. Tumor necrosis factor-alpha (TNF-alpha) is one of the essential cytokines for tumor promotion, and thus, an H. pylori protein that induces TNF-alpha is believed to play a significant role in gastric cancer development in humans. The HP0596 gene product of H. pylori strain 26695 was identified as the TNF-alpha-inducing protein (Tipalpha). Tipalpha is secreted from H. pylori as dimers and enters the gastric cells. It was shown to have a DNA-binding activity. Here, we have determined the crystal structure of Tipalpha from H. pylori. Its monomer consists of two structural domains ("mixed domain" and "helical domain"). Tipalpha exists as a dimer in the crystal, and the dimeric structure represents a novel scaffold for DNA binding. A positively charged surface patch formed across the two monomers of the Tipalpha dimer by the loop between helices alpha1 and alpha2 may be important in DNA binding.

PubMed: 19596016
DOI: 10.1016/j.jmb.2009.07.010

Experimental method

X-RAY DIFFRACTION (2.4 Å)