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Related Experiment Videos

Nitrogenase complexes: multiple docking sites for a nucleotide switch protein.

F Akif Tezcan1, Jens T Kaiser, Debarshi Mustafi

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Mail Code 114-96, Pasadena, CA 91125, USA.

Science (New York, N.Y.)
|August 27, 2005
PubMed
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Adenosine triphosphate (ATP) hydrolysis in nitrogenase drives ammonia production by controlling protein interactions. Different nucleotide states alter protein docking, influencing electron transfer and protein motion in molecular systems.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Nitrogenase is a crucial enzyme complex responsible for converting atmospheric dinitrogen into ammonia.
  • Adenosine triphosphate (ATP) hydrolysis by the Fe-protein is essential for the nitrogenase catalytic cycle.
  • Understanding the structural dynamics of nitrogenase during ATP turnover is key to elucidating its mechanism.

Purpose of the Study:

  • To investigate the conformational changes in the nitrogenase complex during ATP hydrolysis.
  • To identify how different nucleotide states of the Fe-protein influence its interaction with the MoFe-protein.
  • To correlate these structural changes with the regulation of intermolecular electron transfer.

Main Methods:

  • X-ray crystallography was used to determine the structures of the nitrogenase complex in various nucleotide-bound states.

Related Experiment Videos

  • Analysis of distinct crystal structures to identify conformational changes and altered protein-protein interaction interfaces.
  • Examination of the spatial arrangement of redox cofactors in different nucleotide-dependent conformations.

    • Main Results:

    • Crystal structures revealed distinct and mutually exclusive interaction sites on the MoFe-protein surface, dependent on the Fe-protein's nucleotide state.
    • Different docking geometries were observed, leading to nucleotide-state-dependent variations in the distance between redox cofactors.
    • These findings demonstrate that ATP turnover directly influences the relative orientation of the Fe-protein and MoFe-protein.

    Conclusions:

    • ATP hydrolysis in nitrogenase precisely controls the association and dissociation of its protein components through distinct docking geometries.
    • The observed coupling between nucleotide state, docking geometry, and cofactor distance provides a mechanism for regulating intermolecular electron transfer.
    • This principle of nucleotide-driven stabilization of protein-protein interactions may be applicable to other molecular motors and biological systems.