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Structure of the N-terminal domain of Yersinia pestis YopH at 2.0 A resolution

A G Evdokimov1, J E Tropea, K M Routzahn

  • 1Protein Engineering Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, PO Box B, Frederick, MD 21702-1201, USA.

Acta Crystallographica. Section D, Biological Crystallography
|May 26, 2001
PubMed

Insights

Yersinia pestis uses the YopH effector protein to evade host immunity. Researchers determined the crystal structure of YopH's N-terminal domain, revealing a novel fold crucial for bacterial virulence and immune evasion.

Area of Science:

  • Microbiology
  • Structural Biology
  • Immunology

Background:

  • Yersinia pestis causes bubonic plague by injecting effector proteins into host cells.
  • These effectors, like YopH, disrupt host signaling pathways to evade immune responses.
  • YopH has a protein tyrosine phosphatase (PTPase) domain and an N-terminal domain for secretion and target binding.

Purpose of the Study:

  • To determine the crystal structure of the N-terminal domain of Yersinia pestis effector YopH (YopH(N)).
  • To understand the structural basis for YopH secretion, translocation, and substrate recognition.

Main Methods:

  • X-ray crystallography was used to determine the 3D structure of YopH(N) at 2.0 Å resolution.
  • Analysis of the determined structure to identify key functional regions and potential binding sites.

Main Results:

  • The crystal structure of YopH(N) (residues 1-130) was determined.
  • The structure revealed a compact fold with no resemblance to known eukaryotic phosphotyrosine-binding domains.
  • Secretion and translocation signals are integral to the YopH(N) structure.
  • Potential phosphotyrosine-binding residues are clustered, but the recognition mechanism remains unclear.

Conclusions:

  • The N-terminal domain of YopH possesses a unique structural fold essential for its function.
  • The structure provides insights into Yersinia pestis virulence mechanisms and immune evasion strategies.
  • Further studies are needed to elucidate the precise mechanism of phosphotyrosine-protein recognition by YopH(N).

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