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Related Experiment Video

Updated: Jul 19, 2025

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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The structural principles underlying molybdenum insertase complex assembly.

Ahmed H Hassan1,2, Christian Ihling3,4, Claudio Iacobucci3,4,5

  • 1TU Braunschweig, Institute of Plant Biology, Braunschweig, Germany.

Protein Science : a Publication of the Protein Society
|August 12, 2023
PubMed
Summary
This summary is machine-generated.

Molybdenum cofactor (Moco) synthesis requires molybdenum insertase (Mo-insertase). This study models the eukaryotic Cnx1 complex, revealing an asymmetric hexamer that positions its G- and E-domains for efficient Moco formation.

Keywords:
biosynthesis complexmolybdenum cofactormolybdenum insertase

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Trace element molybdenum (Mo) is essential for biological activity, primarily within the nitrogenase-specific FeMo cofactor or the molybdenum cofactor (Moco).
  • Moco comprises an organic molybdopterin (MPT) component and an inorganic Mo-center.
  • Molybdenum insertases (Mo-insertases) catalyze the critical Mo-center formation, featuring distinct G- and E-domains with partially understood functions.

Purpose of the Study:

  • To elucidate the structural and functional relationship between the G- and E-domains of the eukaryotic Mo-insertase Cnx1 complex.
  • To investigate the overall architecture of the Cnx1 complex and its implications for catalytic activity.

Main Methods:

  • Cross-linking mass spectrometry was employed to capture protein-protein interactions within the Cnx1 complex.
  • Computational modeling was utilized to generate a structural model based on the cross-linking data.
  • Analysis focused on the assembly and domain orientation within the eukaryotic Mo-insertase.

Main Results:

  • A structural model of the eukaryotic Cnx1 complex was successfully generated.
  • Cnx1 was revealed to form an asymmetric hexameric complex.
  • The hexameric structure facilitates the alignment of the G- and E-domain active sites into a catalytically productive orientation.

Conclusions:

  • The asymmetric hexameric structure of Cnx1 is crucial for coordinating the sequential steps of molybdenum cofactor synthesis.
  • This structural arrangement optimizes the interaction between the G-domain (MPT adenylation) and E-domain (molybdate insertion) active sites.
  • The findings provide key insights into the mechanism of molybdenum insertion in eukaryotes.