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From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
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Published on: July 4, 2016

Crystal structure of the protease-resistant core domain of Yersinia pestis virulence factor YopR

Florian D Schubot1, Scott Cherry, Brian P Austin

  • 1Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, P.O. Box B, Frederick, MD 21702-1201, USA. waughd@ncifcrf.gov

Protein Science : a Publication of the Protein Society
|June 3, 2005
PubMed

Insights

Yersinia pestis YopR, a virulence factor, was structurally analyzed. Its core domain resembles YopN, suggesting YopR may regulate the type III secretion system (T3SS) during plague infections.

Area of Science:

  • Microbiology
  • Structural Biology
  • Molecular Biology

Background:

  • Yersinia pestis causes plague and uses a type III secretion system (T3SS) to deliver virulence factors into host cells.
  • YopR is a T3SS-secreted factor contributing to Y. pestis virulence, but its function remains largely unknown.

Purpose of the Study:

  • To elucidate the function of Yersinia pestis YopR by determining the crystal structure of its core domain.
  • To investigate potential roles of YopR in the regulation of the type III secretion system.

Main Methods:

  • Determined the crystal structure of the protease-resistant core domain of YopR (residues 38-149).
  • Analyzed the structural features and compared them to known proteins involved in Y. pestis virulence.

Main Results:

  • The YopR core domain comprises five alpha-helices.
  • This structure unexpectedly shares similarity with a domain of YopN, a known regulator of the T3SS in Y. pestis.

Conclusions:

  • The structural similarity between YopR and YopN suggests YopR may be involved in regulating the Y. pestis type III secretion system.
  • Further research is warranted to confirm YopR's role in T3SS regulation during infection.

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