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Related Experiment Videos

Atomic structure of the actin:DNase I complex.

W Kabsch1, H G Mannherz, D Suck

  • 1Max-Planck-Institut für medizinische Forschung, Abteilung Biophysik, Heidelberg, FRG.

Nature
|September 6, 1990
PubMed
Summary
This summary is machine-generated.

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Atomic models reveal rabbit skeletal muscle actin and deoxyribonuclease I structures in ATP and ADP forms. The actin molecule

Area of Science:

  • Biochemistry
  • Structural Biology
  • X-ray Crystallography

Background:

  • Actin is a crucial protein in muscle contraction.
  • Deoxyribonuclease I (DNase I) is an enzyme that interacts with actin.

Purpose of the Study:

  • To determine the atomic structures of the actin-DNase I complex in both ATP and ADP bound states.
  • To elucidate the structural basis of actin-DNase I interaction and nucleotide binding.

Main Methods:

  • X-ray diffraction analysis was employed to determine the atomic models.
  • High-resolution data (2.8 Å and 3 Å) were obtained for the complexes.

Main Results:

  • The atomic models for actin-DNase I complex in ATP and ADP forms were resolved.

Related Experiment Videos

  • Actin comprises two domains, each with two subdomains.
  • Nucleotide (ATP/ADP) and a calcium ion are situated in the cleft between actin domains.

    • Conclusions:

    • The structures of actin in ATP and ADP forms are highly similar.
    • A conserved beta-sheet motif in each actin domain suggests potential gene duplication.
    • The identified beta-sheet topology is similar to that found in hexokinase.