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Related Experiment Videos

Structure of human translin at 2.2 A resolution.

Ikuko Sugiura1, Chiduko Sasaki, Tsukasa Hasegawa

  • 1ZoeGene, 1000 Kamoshida, Aobaku, Yokohama 227-8502, Japan.

Acta Crystallographica. Section D, Biological Crystallography
|March 25, 2004
PubMed
Summary

Human translin protein forms a tetramer structure. Differences in tetramer arrangement between human and mouse translin suggest flexible multimerization, potentially impacting DNA/RNA binding.

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Area of Science:

  • Structural biology
  • Molecular biology
  • Biochemistry

Background:

  • Translin is a protein involved in nucleic acid binding.
  • Understanding protein structure is crucial for elucidating function.

Purpose of the Study:

  • To determine the high-resolution crystal structure of human translin.
  • To compare the quaternary structure of human translin with its murine counterpart.

Main Methods:

  • X-ray crystallography at 2.2 A resolution.
  • Analysis of crystal packing and quaternary structure in space group C222(1).

Main Results:

  • The crystal structure of human translin was determined at 2.2 A resolution.
  • Human translin forms a tetramer in the asymmetric unit.

Related Experiment Videos

  • While monomer structures are similar, human and murine translin tetramers exhibit different relative positions, indicating flexible multimerization.

    • Conclusions:

    • The flexible multimerization of translin may be functionally significant for its interaction with DNA and RNA.
    • Structural insights into human translin provide a basis for further functional studies.