Functional role of the N-terminal domain of bacteriophage T4-gene product 11

A. Y. Vishnevskiy, L. P. Kurochkina, N. N. Sykilinda, N. V. Solov'Eva, M. M. Shneider, Petr Leiman, V. V. Mesyanzhinov

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Bacteriophage T4 late gene product 11 (gp11), the three-dimensional structure of which has been solved by us to 2.0 Å resolution, is a part of the virus' baseplate. The gp11 polypeptide chain consists of 219 amino acid residues and the functionally active protein is a three-domain homotrimer. In this work, we have studied the role of gp11 N-terminal domain in the formation of a functionally active trimer. Deletion variants of gp11 and monoclonal antibodies recognizing the native conformation of gp11 trimer have been selected. Long deletions up to a complete removal of the N-terminal domain, containing 64 residues, do not affect the gp11 trimerization, but considerably change the protein structure and lead to the loss of its ability to incorporate into the baseplate. However, the deletion of the first 17 N-terminal residues results in functionally active protein that can complete the 11 --defective phage particles in in vitro complementation assay. This region of the polypeptide chain is probably essential for gp11-gp10 stable complex formation at the early stages of phage baseplate assembly in vivo. A study of the gp10 deletion variants suggests that the central domain of gp10 trimer is responsible for the interaction with gp11.

Original languageEnglish (US)
Pages (from-to)1111-1118
Number of pages8
JournalBiochemistry (Moscow)
Volume70
Issue number10
DOIs
StatePublished - Oct 2005
Externally publishedYes

Fingerprint

Bacteriophage T4
Bacteriophages
Genes
Peptides
Proteins
Essential Genes
Gene Deletion
Viruses
Monoclonal Antibodies
Conformations
Amino Acids
Assays

Keywords

  • Bacteriophage T4
  • Baseplate
  • Deletion variants
  • Gene product 10
  • Gene product 11
  • Monoclonal antibodies
  • Protein folding

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

Vishnevskiy, A. Y., Kurochkina, L. P., Sykilinda, N. N., Solov'Eva, N. V., Shneider, M. M., Leiman, P., & Mesyanzhinov, V. V. (2005). Functional role of the N-terminal domain of bacteriophage T4-gene product 11. Biochemistry (Moscow), 70(10), 1111-1118. https://doi.org/10.1007/s10541-005-0232-y

Functional role of the N-terminal domain of bacteriophage T4-gene product 11. / Vishnevskiy, A. Y.; Kurochkina, L. P.; Sykilinda, N. N.; Solov'Eva, N. V.; Shneider, M. M.; Leiman, Petr; Mesyanzhinov, V. V.

In: Biochemistry (Moscow), Vol. 70, No. 10, 10.2005, p. 1111-1118.

Research output: Contribution to journalArticle

Vishnevskiy, AY, Kurochkina, LP, Sykilinda, NN, Solov'Eva, NV, Shneider, MM, Leiman, P & Mesyanzhinov, VV 2005, 'Functional role of the N-terminal domain of bacteriophage T4-gene product 11', Biochemistry (Moscow), vol. 70, no. 10, pp. 1111-1118. https://doi.org/10.1007/s10541-005-0232-y
Vishnevskiy AY, Kurochkina LP, Sykilinda NN, Solov'Eva NV, Shneider MM, Leiman P et al. Functional role of the N-terminal domain of bacteriophage T4-gene product 11. Biochemistry (Moscow). 2005 Oct;70(10):1111-1118. https://doi.org/10.1007/s10541-005-0232-y
Vishnevskiy, A. Y. ; Kurochkina, L. P. ; Sykilinda, N. N. ; Solov'Eva, N. V. ; Shneider, M. M. ; Leiman, Petr ; Mesyanzhinov, V. V. / Functional role of the N-terminal domain of bacteriophage T4-gene product 11. In: Biochemistry (Moscow). 2005 ; Vol. 70, No. 10. pp. 1111-1118.
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