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Related Experiment Videos

Granulysin crystal structure and a structure-derived lytic mechanism.

Daniel H Anderson1, Michael R Sawaya, Duilio Cascio

  • 1Howard Hughes Medical Institute, 5-748 MacDonald, Box 951662, Los Angeles, CA 90095-1662, USA. dha@mbi.ucla.edu

Journal of Molecular Biology
|December 19, 2002
PubMed
Summary

Granulysin, a protein from immune cells, can lyse bacterial membranes. Its crystal structure reveals how its charged and hydrophobic regions interact with membranes for bacterial destruction.

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Area of Science:

  • Structural Biology
  • Immunology
  • Biochemistry

Background:

  • Granulysin is a 74-residue basic protein found in human cytolytic T lymphocytes and natural killer cells.
  • It plays a role in the immune response through its lytic activity against target cells, including bacteria.

Purpose of the Study:

  • To determine the crystal structure of granulysin.
  • To elucidate the mechanism by which granulysin lyses bacterial membranes.

Main Methods:

  • Determined the crystal structure of selenomethionyl granulysin using MAD phasing at 2A resolution.
  • Refined the structure model using native diffraction data to 0.96A resolution.
  • Analyzed the distribution of charges, hydrophobic moments, and sulfate ion binding sites.

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Main Results:

  • The crystal structure reveals a five-helical bundle, similar to other saposin folds.
  • Positive charges are distributed around the molecule, with one face being net positive.
  • Sulfate ions bind near the proposed membrane-lytic and hydrophobic segment, suggesting initial membrane interaction orientation.

Conclusions:

  • The structure suggests granulysin lyses bacterial membranes via charge-driven binding and hydrophobic interactions.
  • Crystal packing indicates a potential mechanism for concerted lysis at the cell surface.
  • A proposed hinge motion facilitates membrane insertion and lysis.