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Related Experiment Videos

Structure and function of a squalene cyclase

K U Wendt1, K Poralla, G E Schulz

  • 1Institut für Organische Chemie und Biochemie, Albertstrasse 21, D-79104 Freiburg im Breisgau, Germany.

Science (New York, N.Y.)
|September 20, 1997
PubMed
Summary
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The crystal structure of Alicyclobacillus acidocaldarius squalene-hopene cyclase was determined. This enzyme is structurally and mechanistically similar to human cholesterol biosynthesis enzymes, offering insights into their function.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Squalene-hopene cyclase (ShC) from Alicyclobacillus acidocaldarius shares mechanistic and sequence similarities with 2,3-oxidosqualene cyclases (OSCs) involved in cholesterol biosynthesis.
  • The determined structure reveals ShC as a membrane protein with characteristics akin to prostaglandin-H2 synthase.
  • Understanding ShC provides insights into the broader family of cyclases, including those crucial for human health.

Purpose of the Study:

  • To determine the high-resolution crystal structure of squalene-hopene cyclase from Alicyclobacillus acidocaldarius.
  • To elucidate the structural basis for its enzymatic mechanism and its relationship to human OSCs.
  • To characterize its membrane-binding properties and active site architecture.

Main Methods:

Related Experiment Videos

  • X-ray crystallography at 2.9 angstrom resolution.
  • Structural analysis of the enzyme's active site and surface features.
  • Bioinformatic comparison with related cyclases.

Main Results:

  • The crystal structure of Alicyclobacillus acidocaldarius squalene-hopene cyclase was resolved to 2.9 angstroms.
  • The enzyme exhibits membrane-binding characteristics similar to prostaglandin-H2 synthase.
  • A large central cavity lined with aromatic residues forms the active site, suitable for squalene binding.
  • A proposed catalytic mechanism involves an aspartate-histidine pair initiating protonation.

Conclusions:

  • The structure of squalene-hopene cyclase provides a detailed molecular model for this class of enzymes.
  • Its similarity to human cholesterol biosynthesis enzymes suggests conserved structural and mechanistic principles.
  • The QW-motifs on the surface may play a role in stabilizing the protein during catalysis.