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Structure of human translin at 2.2 A resolution
Ikuko Sugiura1, Chiduko Sasaki, Tsukasa Hasegawa
1ZoeGene, 1000 Kamoshida, Aobaku, Yokohama 227-8502, Japan.
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.
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.
- 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.