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ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
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Structural Basis of Bifunctional CTP/dCTP Synthase.

Chen-Jun Guo1, Zherong Zhang2, Jia-Li Lu1

  • 1School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.

Journal of Molecular Biology
|August 22, 2024
PubMed
Summary

Cytidine triphosphate synthase (CTPS) binds both ribonucleotides and deoxyribonucleotides, forming filaments. This study reveals the structural basis for CTPS

Keywords:
CTP synthaseCTP/dCTP synthasecryo-electron microscopycytoophidiumfilamentation

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Cytidine 5'-triphosphate synthase (CTPS) catalyzes the final step in de novo CTP synthesis.
  • CTPS forms cytoophidia across all domains of life and binds ribonucleotides (NTPs) to form filaments.
  • Previous studies indicated CTPS binds deoxyribonucleotides (dNTPs) to produce dCTP, but the structural basis was unknown.

Purpose of the Study:

  • To elucidate the structural basis of CTPS binding to dNTPs.
  • To compare the binding and reaction characteristics of NTPs and dNTPs with CTPS.
  • To investigate the bifunctional activity of CTPS as both CTP and dCTP synthase.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to resolve the structure of Drosophila melanogaster CTPS bound to dNTPs.
  • Biochemical analysis to compare NTP and dNTP binding and reaction characteristics.
  • Structural determination at a resolution of 2.7 Å.

Main Results:

  • Drosophila CTPS forms filaments with dNTPs, similar to its interaction with NTPs.
  • The study resolved the structure of CTPS bound to dNTPs.
  • CTPS exhibits bifunctional activity, acting as both CTP and dCTP synthase in vitro.

Conclusions:

  • The same enzyme, CTPS, can synthesize both CTP and dCTP.
  • Structural and biochemical data provide a basis for CTPS's dual enzymatic activity.
  • This bifunctionality offers new insights into nucleotide synthesis regulation.