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Updated: May 18, 2026

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
14:58

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

Structure of the GcpE (IspG)-MEcPP complex from Thermus thermophilus

Ingo Rekittke1, Hassan Jomaa, Ulrich Ermler

  • 1Institut für Klinische Immunologie und Transfusionsmedizin, Justus-Liebig-Universität Giessen, Giessen, Germany.

FEBS Letters
|September 13, 2012
PubMed

Insights

The methylerythritol phosphate (MEP) pathway is crucial for pathogen survival. This study reveals the structure of HMBPP synthase (GcpE) bound to MEcPP, offering insights into MEP pathway inhibition.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Isoprenoid precursors are vital biomolecules synthesized via the mevalonate pathway (humans) or methylerythritol phosphate (MEP) pathway (pathogens).
  • The MEP pathway enzyme HMBPP synthase (GcpE), containing an iron-sulfur cluster, catalyzes the conversion of MEcPP to HMBPP.

Purpose of the Study:

  • To elucidate the catalytic mechanism of GcpE.
  • To provide a structural basis for designing inhibitors targeting the MEP pathway in human pathogens.

Main Methods:

  • X-ray crystallography of the Thermus thermophilus GcpE-MEcPP complex at 1.55Å resolution.

Main Results:

  • The crystal structure reveals MEcPP binding induces domain rotation, positioning the [4Fe-4S] cluster near the TIM-barrel entrance.
  • The apical iron of the [4Fe-4S] cluster directly interacts with the C3 oxygen atom of MEcPP.

Conclusions:

  • The structural data illuminates the GcpE catalytic mechanism.
  • This provides a foundation for structure-based drug design against essential microbial pathways.

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