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An intact conformation at the tip of elongation factor G domain IV is functionally important

Academic Article
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Overview

authors

  • Martemyanov, Kirill
  • Yarunin, A. S.
  • Liljas, A.
  • Gudkov, A. T.

publication date

  • August 1998

journal

  • FEBS Letters  Journal

abstract

  • Three variants of Thermus thermophilus EF-G with mutations in the loop at the distal end of its domain IV were obtained. The replacement of His-573 by Ala and double mutation H573A/D576A did not influence the functional activity of EF-G. On the other hand, the insertion of six amino acids into the loop between residues Asp-576 and Ser-577 reduced the translocational activity of EF-G markedly, while its GTPase activity was not affected. It is concluded that the native conformation of the loop is important for the factor-promoted translocation in the ribosome. The functional importance of the entire EF-G domain IV is discussed.

subject areas

  • GTP Phosphohydrolase-Linked Elongation Factors
  • Mutation
  • Peptide Elongation Factor G
  • Peptide Elongation Factors
  • Protein Conformation
  • Structure-Activity Relationship
  • Thermus thermophilus
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Research

keywords

  • elongation factor G function
  • mutagenesis
  • ribosome
  • translocation
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Identity

International Standard Serial Number (ISSN)

  • 0014-5793

Digital Object Identifier (DOI)

  • 10.1016/s0014-5793(98)00982-x

PubMed ID

  • 9738479
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Additional Document Info

start page

  • 205

end page

  • 208

volume

  • 434

issue

  • 1-2

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