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Related Experiment Videos

Enzyme-mononucleotide interactions: three different folds share common structural elements for ATP recognition.

K A Denessiouk1, J V Lehtonen, M S Johnson

  • 1Department of Biochemistry and Pharmacy, Abo Akademi University, Turku, Finland.

Protein Science : a Publication of the Protein Society
|March 19, 1999
PubMed
Summary

Three unrelated ATP-dependent enzymes share a common ATP-binding site organization. This convergent evolution highlights how different protein folds can achieve similar local structures for essential functions like ATP binding.

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ADAPTATION AND RULES OF FORM: CHIRALITY AND SHAPE IN PARTULA SUTURALIS.

Evolution; international journal of organic evolution·2017

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Evolution

Background:

  • ATP-dependent enzymes are crucial for numerous cellular processes.
  • Understanding the structural basis of ATP binding is key to enzyme function.
  • Diverse enzymes often exhibit conserved functional mechanisms despite differing folds.

Purpose of the Study:

  • To investigate the structural similarities in ATP-binding sites across unrelated ATP-dependent enzymes.
  • To identify conserved residues and structural motifs involved in ATP binding.
  • To explore the role of convergent evolution in enzyme function.

Main Methods:

  • Comparative structural analysis of ATP-binding sites.
  • Identification of structurally equivalent residues across different enzyme families.

Related Experiment Videos

  • Analysis of hydrogen bonding and hydrophobic interactions within the ATP-binding pocket.
  • Main Results:

    • Three distinct ATP-dependent enzymes (cAMP-dependent protein kinase, D-Ala:D-Ala ligase, and alpha2beta2 ribonucleotide reductase alpha-subunit) exhibit a conserved organization of their ATP-binding sites.
    • A core set of 23 structurally equivalent residues, including beta-sheet strands and a loop, form the common binding motif.
    • Key hydrogen bonds involving four conserved amino acids orient the adenine moiety of ATP, and a conserved lysine residue anchors the alpha-phosphate.

    Conclusions:

    • Convergent evolution has led to similar local structures for ATP binding in unrelated proteins.
    • Nature utilizes conserved structural fragments to achieve functional requirements, such as efficient ATP binding.
    • This study provides insights into the principles of protein structure and function, demonstrating how different evolutionary paths can converge on optimal solutions.