TY - JOUR
T1 - Fluoroaluminates do not affect the guanine‐nucleotide binding centre of the peptide chain elongation factor EF‐Tu
AU - KRAAL, Barend
AU - de GRAAF, J. Martien
AU - MESTERS, Jeroen R.
AU - van HOOF, Peter J.M.
AU - JACQUET, Eric
AU - PARMEGGIANI, Andrea
N1 - Copyright:
Copyright 2016 Elsevier B.V., All rights reserved.
PY - 1990/9
Y1 - 1990/9
N2 - 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 AIF−4 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.
AB - 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 AIF−4 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.
UR - http://www.scopus.com/inward/record.url?scp=0025152832&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1990.tb19228.x
DO - 10.1111/j.1432-1033.1990.tb19228.x
M3 - Journal articles
C2 - 2209587
AN - SCOPUS:0025152832
SN - 0014-2956
VL - 192
SP - 305
EP - 309
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 2
ER -