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Transformation of a Fragment of β-Structural Bacteriophage T4 Adhesin to Stable α-Helical Trimer

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Abstract

Gene product 12 of bacteriophage T4, adhesin, serves to adhere the virus to host cells. Adhesin is a fibrous homotrimer, and a novel tertiary structure element, a β-helix, is supposed to be a major structural feature of this protein. We have constructed two truncated gp12 mutants, 12N1 and 12N2, containing 221 and 135 N-terminal residues, respectively. When expressed in E. coli cells, these gp12 fragments formed labile β-structural trimers. Another hybrid protein, 12FN, containing 179 N-terminal amino acid residues of gp12 fused to the C-terminal domain (31 amino acids) of T4 fibritin, was shown to have a trimeric proteolytically resistant a-helical structure. This structure is probably similar to that of fibritin, which has a triple α-helical coiled-coil structure. Hence, we have demonstrated the possibility of global transformation of fibrous protein structure using fusion with a C-terminal domain that initiates trimerization.

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Authors and Affiliations

  1. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, Moscow, 117071, Russia

    K. A. Miroshnikov

  2. Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117871, Russia; fax

    N. V. Sernova & M. M. Shneider

  3. Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117871, Russia; fax

    V. V. Mesyanzhinov

Authors
  1. K. A. Miroshnikov
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  2. N. V. Sernova
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  3. M. M. Shneider
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  4. V. V. Mesyanzhinov
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Miroshnikov, K.A., Sernova, N.V., Shneider, M.M. et al. Transformation of a Fragment of β-Structural Bacteriophage T4 Adhesin to Stable α-Helical Trimer. Biochemistry (Moscow) 65, 1346–1351 (2000). https://doi.org/10.1023/A:1002888419749

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