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Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4 Å resolution

Nature Structural Biology volume 4, pages 153–157 (1997)Cite this article

Abstract

We solved the crystal structure of the homotetrameric single-stranded DNA binding (SSB) protein from human mitochondria at a resoluntion of 2.4 Å. The tetramer is formed by two dimers interacting head-to-head and shows D2 symmetry. Sequence-related tetrameric SSB proteins occur in prokaryotes and eukaryotic mitochondria; this is the first report of an atomic resolution structure of this type of protein. Using biochemical data and analysis of sequence homologies, we were able to correlate the functional properties with structure. We propose that ssDNA wraps around the tetrameric HsmtSSB protein through electropositive channels guided by flexible loops.

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Authors and Affiliations

  1. Department of Biochemistry and Biophysics, Washington State University, Pullman, Washington, 99164-4660, USA

    Cheng Yang & ChulHee Kang

  2. Department of Biophysical Chemistry, Hannover Medical School, 30623, Hannover, Germany

    Ute Curth & Claus Urbanke

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  1. Cheng Yang
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  2. Ute Curth
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  3. Claus Urbanke
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  4. ChulHee Kang
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Yang, C., Curth, U., Urbanke, C. et al. Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4 Å resolution. Nat Struct Mol Biol 4, 153–157 (1997). https://doi.org/10.1038/nsb0297-153

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