Fluoroaluminates do not affect the guanine‐nucleotide binding centre of the peptide chain elongation factor EF‐Tu

Barend KRAAL*, J. Martien de GRAAF, Jeroen R. MESTERS, Peter J.M. van HOOF, Eric JACQUET, Andrea PARMEGGIANI

*Corresponding author for this work
11 Citations (Scopus)

Abstract

EF‐Tu is often referred to as a model for guanine‐nucleotide‐binding regulatory proteins (G‐proteins), since X‐ray diffraction analysis of its GTP‐binding domain shows a detailed location of the ‘consensus’ amino acid sequences involved in nucleotide binding. Fluoroaluminates are thought to mimick the γ‐phosphate in the GTPase centre on account of their activating effect on a variety of GTP binding proteins. In the case of EF‐Tu, we could find no such effects on the basis of at least three independent functional assays. We did notice, however, complicating interactions between free nucleotides, fluoroaluminates and other ligands. By consequence, if indeed AIF4 behaves as a γ‐phosphate analogue in G‐proteins, then EF‐Tu must have a different GDP/GTP binding site, despite of the conserved consensus sequences.

Original languageEnglish
JournalEuropean Journal of Biochemistry
Volume192
Issue number2
Pages (from-to)305-309
Number of pages5
ISSN0014-2956
DOIs
Publication statusPublished - 09.1990

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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