Native ESI-MS and Collision Induced Unfolding (CIU) of the Complex between Bacterial Elongation Factor-Tu and the Antibiotic Enacyloxin IIa
Publication Date
June 3, 2024
Creators
Description
Raw native-MS and IM-MS data supporting publication in JASMS.
Abstract:
Collision induced unfolding (CIU) of protein ions, monitored by ion mobility-mass spectrometry (IM-MS), can be used to assess the stability of their compact gas-phase fold, and hence provide structural information. The bacterial elongation factor EF-Tu, a key protein for protein translation in prokaryotes, and hence a promising antibiotic target, has been studied by CIU. The major [M+12H]12+ ion of EF-Tu unfolded in collision with Ar atoms between 40 and 50 V, corresponding to an Elab energy of 480-500 eV. Binding of the cofactor analogue GDPNP and the antibiotic enacyloxin IIa stabilized the compact fold of EF-Tu, although dissociation of the latter from the complex diminished its stabilizing effect at higher collision energies
Associate publ. DOI
Subjects
Subjects (JACS)
Subjects (LC)
Divisions
University of Nottingham, UK Campus::Faculty of Science::School of Chemistry
Data type
Mass Spectrometry Data Files
Grant Number
BB/T008369/1
Data collection method
Waters Synapt G1 HDMS High Definition Mass Spectrometer
Resource languages
English
Publisher
The University of Nottingham
Date Issued
June 3, 2024
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Name
MS_RAW_DATA.zip
Description
All Raw Mass Spectrometry Data
Size
345.06 MB
Format
Unknown
Checksum (MD5)
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