Abstract
Trigger factor (TF) is a multi-domain molecular chaperone that binds to the bacterial ribosome at the tunnel exit from which nascent polypeptides emerge. We present here the NMR assignments of the ribosome binding domain (RBD) of TF from Escherichia coli as a stable 26 kDa dimer, using conditions that are similar to a crystallographic study from which an X-ray crystal structure of the identical construct was determined.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Carbon Isotopes / chemistry
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Escherichia coli / chemistry*
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Escherichia coli Proteins / chemistry*
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Magnetic Resonance Spectroscopy / methods*
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Nitrogen Isotopes / chemistry
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Peptidylprolyl Isomerase / chemistry*
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Protein Binding
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Protons
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Ribosome Subunits, Small, Bacterial / chemistry*
Substances
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Carbon Isotopes
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Escherichia coli Proteins
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Nitrogen Isotopes
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Protons
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trigger factor, E coli
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Peptidylprolyl Isomerase