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The dynamic dimer structure of the chaperone Trigger Factor

Artikel i vetenskaplig tidskrift
Författare L. Morgado
Björn Marcus Burmann
T. Sharpe
A. Mazur
S. Hiller
Publicerad i Nature Communications
Volym 8
Nummer/häfte 1
ISSN 20411723 (ISSN)
Publiceringsår 2017
Publicerad vid Institutionen för kemi och molekylärbiologi
Språk en
Länkar dx.doi.org/10.1038/s41467-017-02196...
Ämnesord alanine, chaperone, dimer, peptidylprolyl isomerase, potassium chloride, trigger factor, unclassified drug, cells and cell components, coliform bacterium, cytology, nuclear magnetic resonance, physiology, protein, spectroscopy, substrate, aqueous solution, Article, binding affinity, binding site, biophysics, chemical structure, conformational transition, Escherichia coli, molecular dynamics, nonhuman, nuclear magnetic resonance spectroscopy, protein analysis, protein interaction, protein structure, ribosome, structure analysis
Ämneskategorier Molekylärbiologi

Sammanfattning

The chaperone Trigger Factor (TF) from Escherichia coli forms a dimer at cellular concentrations. While the monomer structure of TF is well known, the spatial arrangement of this dimeric chaperone storage form has remained unclear. Here, we determine its structure by a combination of high-resolution NMR spectroscopy and biophysical methods. TF forms a symmetric head-to-tail dimer, where the ribosome binding domain is in contact with the substrate binding domain, while the peptidyl-prolyl isomerase domain contributes only slightly to the dimer affinity. The dimer structure is highly dynamic, with the two ribosome binding domains populating a conformational ensemble in the center. These dynamics result from intermolecular in trans interactions of the TF client-binding site with the ribosome binding domain, which is conformationally frustrated in the absence of the ribosome. The avidity in the dimer structure explains how the dimeric state of TF can be monomerized also by weakly interacting clients. © 2017 The Author(s).

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