TRANSFERRED NUCLEAR OVERHAUSER EFFECT SPECTROSCOPY STUDY OF A PEPTIDEFROM THE PAPG PILUS SUBUNIT BOUND BY THE ESCHERICHIA-COLI PAPD CHAPERONE

Interaction of the Escherichia coli PapD chaperone with the synthetic peptide PapG308-314 (Thr-Met-Val-Leu-Ser-Phe-Pro), corresponding to th e seven C-terminal residues of the PapG pilus subunit, was studied by transferred nuclear Overhauser effect (TRNOE) spectroscopy. The observ ation of cross-peaks corresponding to either intraresidue or sequentia l (CH)-H-alpha/NHi+1 and (CH)-H-beta/NH TRNOEs and the absence of sequ ential NHi\NHi+1 TRNOEs indicate that the peptide binds to PapD in an extended conformation, In addition, line-broadening effects gave infor mation of the peptide's mode of interaction with PapD, These observati ons were in excellent agreement with a recent crystal structure of a P apG peptide complexed with PapD. (C) 1997 Federation of European Bioch emical Societies.