The Structure of Helicobacter pylori HP0310 Reveals an Atypical Peptidoglycan Deacetylase
2011

Structure of Helicobacter pylori Peptidoglycan Deacetylase

publication Evidence: moderate

Author Information

Author(s): Shaik Md Munan, Cendron Laura, Percudani Riccardo, Zanotti Giuseppe

Primary Institution: Department of Biological Chemistry, University of Padua, Padua, Italy

Hypothesis

What is the structure and function of the peptidoglycan deacetylase HP0310 from Helicobacter pylori?

Conclusion

The study reveals that HP0310 does not exhibit activity on typical polysaccharide substrates, suggesting it may bind a small molecule instead.

Supporting Evidence

  • HP0310 was over-expressed under oxidative stress conditions.
  • HP0310 knock-out mutants showed increased susceptibility to lysozyme degradation.
  • Expression of HP0310 was induced when H. pylori was in contact with macrophages.

Takeaway

Scientists studied a protein from a bacteria that helps it avoid the immune system, but they found it doesn't work like similar proteins.

Methodology

The enzyme was cloned, expressed, purified, crystallized, and its structure was determined through X-ray crystallography.

Limitations

The specific substrate of HpPgdA has yet to be identified, and the enzyme showed no activity on tested polysaccharide substrates.

Digital Object Identifier (DOI)

10.1371/journal.pone.0019207

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