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Crystal structure of the Yersinia type III secretion protein YscE

Jason Phan1, Brian P Austin, David S Waugh

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

Protein Science : a Publication of the Protein Society
|October 1, 2005
PubMed

Insights

The plague bacterium Yersinia pestis uses a type III secretion system (T3SS) to inject toxins into host cells. Researchers determined the structure of YscE, a key T3SS protein, revealing it forms a dimer.

Area of Science:

  • Microbiology
  • Structural Biology
  • Molecular Biology

Background:

  • * Yersinia pestis causes plague by injecting virulence factors into host cells using a type III secretion system (T3SS).
  • * The T3SS is a complex apparatus comprising numerous Yersinia secretion (Ysc) proteins.
  • * Understanding the structure of individual Ysc proteins is crucial for elucidating T3SS function.

Purpose of the Study:

  • * To determine the three-dimensional structure of YscE, the smallest component of the Yersinia T3SS apparatus.
  • * To investigate the oligomeric state and potential assembly mechanism of YscE.

Main Methods:

  • * Primarily utilized X-ray crystallography to resolve the structure of YscE.
  • * Employed analytical ultracentrifugation to assess the oligomeric state of YscE in solution.

Main Results:

  • * The crystal structure of YscE was determined, revealing its molecular architecture.
  • * YscE was found to exist as a dimer in solution, indicating a specific oligomeric state.
  • * The structural data provides insights into the probable mode of YscE oligomerization within the T3SS.

Conclusions:

  • * YscE, a small but essential T3SS component, forms a stable dimer.
  • * The dimeric structure of YscE likely plays a role in the assembly and function of the type III secretion apparatus.
  • * Further structural and functional studies of YscE oligomerization will enhance our understanding of Yersinia virulence mechanisms.

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