1H, 15N and 13C assignments of the dimeric ribosome binding domain of trigger factor from Escherichia coli.
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.
Hsu
Shang-Te Danny
ST
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK. stdh2@cam.ac.uk
Dobson
Christopher M
CM
D001665:Binding Sites; D002247:Carbon Isotopes / Q000737:chemistry; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009587:Nitrogen Isotopes / Q000737:chemistry; D019696:Peptidylprolyl Isomerase / Q000737:chemistry*; D011485:Protein Binding; D011522:Protons; D054680:Ribosome Subunits, Small, Bacterial / Q000737:chemistry*
D002247:Carbon Isotopes; D029968:Escherichia coli Proteins; D009587:Nitrogen Isotopes; D011522:Protons; C403324:trigger factor, E coli; D019696:Peptidylprolyl Isomerase