scholarly journals Crystal structure of toxin HP0892 from Helicobacter pylori with two Zn(II) at 1.8 Å resolution

2014 ◽  
Vol 23 (6) ◽  
pp. 819-832 ◽  
Author(s):  
Hookang Im ◽  
Sun-Bok Jang ◽  
Chinar Pathak ◽  
Yeon-Jin Yang ◽  
Hye-Jin Yoon ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Helicobacter Pylori

scholarly journals Structural Analysis of Variability and Interaction of the N-terminal of the Oncogenic Effector CagA of Helicobacter pylori with Phosphatidylserine

2018 ◽  
Vol 19 (10) ◽  
pp. 3273 ◽  
Author(s):  
Cindy Ulloa-Guerrero ◽  
Maria Delgado ◽  
Carlos Jaramillo
Keyword(s):  
Crystal Structure ◽  
Helicobacter Pylori ◽  
Conservation Score ◽  
Intermolecular Forces ◽  
P Value ◽  
Cytotoxin Associated Gene A ◽  
Molecular Forces ◽  
Severe Pathology ◽  
Risk Of Cancer ◽  
Bulk Effect

Helicobacter pylori cytotoxin-associated gene A protein (CagA) has been associated with the increase in virulence and risk of cancer. It has been demonstrated that CagA’s translocation is dependent on its interaction with phosphatidylserine. We evaluated the variability of the N-terminal CagA in 127 sequences reported in NCBI, by referring to molecular interaction forces with the phosphatidylserine and the docking of three mutations chosen from variations in specific positions. The major sites of conservation of the residues involved in CagA–Phosphatidylserine interaction were 617, 621 and 626 which had no amino acid variation. Position 636 had the lowest conservation score; mutations in this position were evaluated to observe the differences in intermolecular forces for the CagA–Phosphatidylserine complex. We evaluated the docking of three mutations: K636A, K636R and K636N. The crystal and mutation models presented a ΔG of −8.919907, −8.665261, −8.701923, −8.515097 Kcal/mol, respectively, while mutations K636A, K636R, K636N and the crystal structure presented 0, 3, 4 and 1 H-bonds, respectively. Likewise, the bulk effect of the ΔG and amount of H-bonds was estimated in all of the docking models. The type of mutation affected both the ΔG ( χ 2 ( 1 ) = 93.82 , p-value < 2.2 × 10 − 16 ) and the H-bonds ( χ 2 ( 1 ) = 91.93 , p-value < 2.2 × 10 − 16 ). Overall, 76.9% of the strains that exhibit the K636N mutation produced a severe pathology. The average H-bond count diminished when comparing the mutations with the crystal structure of all the docking models, which means that other molecular forces are involved in the CagA–Phosphatidylserine complex interaction.

scholarly journals Crystal structure of JHP933 from Helicobacter pylori J99

2014 ◽  
Vol 70 (a1) ◽  
pp. C823-C823
Author(s):  
Sang Jae Lee ◽  
Ji Young Yoon ◽  
Bong-Jin Lee ◽  
Se Won Suh
Keyword(s):  
Crystal Structure ◽  
Helicobacter Pylori ◽  
Peptic Ulcer ◽  
Functional Characterization ◽  
Domain Architecture ◽  
Structural Similarity ◽  
Terminal Domain ◽  
Plasticity Region ◽  
H Pylori ◽  
And Function

Helicobacter pylori infection is the main cause of chronic gastritis, gastric mucosal atrophy, peptic ulcer, and some forms of gastric cancer. There has been considerable interest in strain-specific genes found outside of the cag pathogenicity island, especially genes in the plasticity regions of H. pylori. In H. pylori strain J99, the plasticity region contains 48 genes ranging from jhp0914 to jhp0961. Because little is known about many of these genes in the plasticity region, further studies are necessary to elucidate their roles in H. pylori-associated pathogenesis. The JHP933 protein, encoded by the jhp0933 gene in the plasticity region of H. pylori J99, is one of the prevalently expressed proteins in some gastritis and peptic ulcer patients. However, its structure and function remain unknown. Here, we have determined the crystal structure of JHP933, revealing the first two-domain architecture of DUF1814 family. The N-terminal domain has the nucleotidyltransferase fold and the C-terminal domain is a helix bundle. Structural similarity of JHP933 to known nucleotidyltransferases is very remote, suggesting that it may function as a novel nucleotidyltransferase. It is expected that this study will facilitate functional characterization of JHP933 to obtain an insight into its role in pathogenesis by the H. pylori plasticity region.

Crystal structure of truncated FlgD from the human pathogen Helicobacter pylori

2016 ◽  
Vol 194 (2) ◽  
pp. 147-155 ◽  
Author(s):  
Ivana Pulić ◽  
Laura Cendron ◽  
Marco Salamina ◽  
Patrizia Polverino de Laureto ◽  
Dubravka Matković-Čalogović ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Helicobacter Pylori ◽  
Human Pathogen

The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension

2008 ◽  
Vol 1784 (11) ◽  
pp. 1601-1606 ◽  
Author(s):  
Luciana Esposito ◽  
Anke Seydel ◽  
Rosa Aiello ◽  
Giosué Sorrentino ◽  
Laura Cendron ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Superoxide Dismutase ◽  
Helicobacter Pylori

scholarly journals Crystal structure of the type II 3-dehydroquinase from Helicobacter pylori

2003 ◽  
Vol 51 (4) ◽  
pp. 616-617 ◽  
Author(s):  
Byung Il Lee ◽  
Je Eun Kwak ◽  
Se Won Suh
Keyword(s):  
Crystal Structure ◽  
Helicobacter Pylori ◽  
Type Ii

Crystal structure of apo and copper bound HP0894 toxin from Helicobacter pylori 26695 and insight into mRNase activity

2013 ◽  
Vol 1834 (12) ◽  
pp. 2579-2590 ◽  
Author(s):  
Chinar Pathak ◽  
Hookang Im ◽  
Yeon-Jin Yang ◽  
Hye-Jin Yoon ◽  
Hong-Man Kim ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Helicobacter Pylori ◽  
Insight Into

Crystal Structure of Hypothetical Protein HP0062 (O24902_HELPY) from Helicobacter pylori at 1.65 A Resolution

2009 ◽  
Vol 146 (4) ◽  
pp. 535-540 ◽  
Author(s):  
S.-B. Jang ◽  
A.-R. Kwon ◽  
W.-S. Son ◽  
S. J. Park ◽  
B.-J. Lee
Keyword(s):  
Crystal Structure ◽  
Helicobacter Pylori ◽  
Hypothetical Protein

Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter pylori

2005 ◽  
Vol 1753 (2) ◽  
pp. 240-246 ◽  
Author(s):  
Elena Papinutto ◽  
Henry J. Windle ◽  
Laura Cendron ◽  
Roberto Battistutta ◽  
Dermot Kelleher ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Helicobacter Pylori ◽  
Alkyl Hydroperoxide Reductase ◽  
Alkyl Hydroperoxide
Sign in / Sign up

Export Citation Format

Share Document