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Related Experiment Videos

Latent LytM at 1.3A resolution.

Sergey G Odintsov1, Izabela Sabala, Malgorzata Marcyjaniak

  • 1International Institute of Molecular and Cell Biology, ul. Trojdena 4, 02-109 Warsaw, Poland.

Journal of Molecular Biology
|December 23, 2003
PubMed
Summary
This summary is machine-generated.

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The crystal structure of Staphylococcus aureus LytM reveals a latent enzyme form. Truncated LytM shows higher activity, suggesting a proenzyme mechanism similar to other metallopeptidases.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • LytM is a Zn(2+)-dependent glycyl-glycine endopeptidase from Staphylococcus aureus.
  • It belongs to the lysostaphin-type metallopeptidase family (MEROPS M23/37) and possesses a conserved HxH motif.

Purpose of the Study:

  • To determine the crystal structure of LytM, the first of its kind for a lysostaphin-type peptidase.
  • To investigate the enzyme's active site and potential regulatory mechanisms.

Main Methods:

  • 1.3Å resolution crystal structure determination of LytM.
  • Biochemical assays comparing full-length and truncated LytM activity.

Main Results:

  • The crystal structure shows Zn(2+) coordinated by N117, H210, D214, and H293, with H291 not directly involved in coordination.

Related Experiment Videos

  • The absence of a water molecule in the Zn(2+) coordination sphere suggests a latent enzyme state.
  • A truncated LytM lacking N117 exhibits significantly higher specific activity than the full-length enzyme.

    • Conclusions:

    • The LytM crystal structure represents a latent form, potentially regulated by an "asparagine switch" analogous to the "cysteine switch" in metalloproteases.
    • LytM likely functions as a proenzyme, with N-terminal processing required for full activity, consistent with observations in related enzymes and bacterial supernatants.