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Characterization of Surface Topology and Binding Area in Complexes of the Elongation Factor Proteins EF‐Ts and EF‐Tu⋅GDP from Thermus thermophilus : A Study by Protein Chemical Modification and Mass Spectrometry
Author(s) -
Glocker Michael O.,
Nock Steffen,
Sprinzl Mathias,
Przybylski Michael
Publication year - 1998
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/(sici)1521-3765(19980416)4:4<707::aid-chem707>3.0.co;2-c
Subject(s) - acetylation , chemistry , elongation factor , lysine , elongation , peptide , mass spectrometry , characterization (materials science) , biochemistry , amino acid , chromatography , materials science , nanotechnology , ribosome , rna , ultimate tensile strength , metallurgy , gene
The characterization of protein–protein interactions by means of amino acetylation of lysine residues in combination with mass‐spectrometric peptide mapping is described. The differential acetylation pattern for the free proteins (elongation factors EF‐Tu and EF‐Ts) and the EF‐Tu⋅EF‐Ts complex was used to characterize structural changes in the effector loop of EF‐Tu, and to identify the N ‐terminal domain of EF‐Ts as the major interacting area. The Lys‐45 and Lys‐52 residues in EF‐Tu (shown right) and Lys‐21 and Lys‐45 residues of EF‐Ts were found to be completely shielded from acetylation as a result of complex formation.