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Protein farnesyltransferase: structure and implications for substrate binding

P Dunten1, U Kammlott, R Crowther

  • 1Roche Research Center, Hoffmann-La Roche Inc., Nutley, New Jersey 07110, USA.

Biochemistry
|June 12, 1998
PubMed
Summary
This summary is machine-generated.

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Researchers determined the rat protein farnesyltransferase crystal structure, revealing a novel substrate binding model. This model differs from previous proposals and explains key mutation effects on enzyme activity.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Farnesyltransferase is a crucial enzyme in protein prenylation.
  • Understanding its structure is key to developing targeted inhibitors.
  • Previous structural models for substrate binding existed but required further refinement.

Purpose of the Study:

  • To elucidate the three-dimensional crystal structure of rat protein farnesyltransferase.
  • To propose a refined model for substrate binding and enzyme catalysis.
  • To reconcile structural data with existing mutation studies.

Main Methods:

  • X-ray crystallography was employed to solve the protein structure.
  • Multiple isomorphous replacement methods were utilized.
  • High-resolution (2.75 A) structural data was obtained.

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Main Results:

  • The crystal structure of rat farnesyltransferase was determined.
  • A novel model for farnesyl diphosphate and peptide substrate binding was proposed.
  • The model highlights the role of Arg202 in peptide substrate binding.
  • Observed electron density suggested bound farnesyl diphosphate in the active site.

Conclusions:

  • The proposed substrate binding model differs from prior hypotheses.
  • The structural model provides a basis for understanding enzyme specificity and catalysis.
  • This work offers insights into the mechanism of farnesyltransferase.