Transferred nuclear Overhauser effect spectroscopy study of a peptide from the PapG pilus subunit bound by the Escherichia coli PapD chaperone

FEBS Lett. 1997 Jul 21;412(1):115-20. doi: 10.1016/s0014-5793(97)00759-x.

Abstract

Interaction of the Escherichia coli PapD chaperone with the synthetic peptide PapG308-314 (Thr-Met-Val-Leu-Ser-Phe-Pro), corresponding to the seven C-terminal residues of the PapG pilus subunit, was studied by transferred nuclear Overhauser effect (TRNOE) spectroscopy. The observation of cross-peaks corresponding to either intraresidue or sequential C(alpha)H/NH and C(beta)H/NH TRNOEs and the absence of sequential NH(i)/NH(i+1) TRNOEs indicate that the peptide binds to PapD in an extended conformation. In addition, line-broadening effects gave information of the peptide's mode of interaction with PapD. These observations were in excellent agreement with a recent crystal structure of a PapG peptide complexed with PapD.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Escherichia coli / chemistry*
  • Adhesins, Escherichia coli / metabolism
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Crystallization
  • Escherichia coli / chemistry*
  • Escherichia coli Proteins*
  • Fimbriae Proteins*
  • Fimbriae, Bacterial*
  • Magnetic Resonance Spectroscopy*
  • Models, Molecular
  • Molecular Chaperones*
  • Molecular Structure
  • Periplasmic Proteins*
  • Protein Conformation

Substances

  • Adhesins, Escherichia coli
  • Bacterial Proteins
  • Escherichia coli Proteins
  • Molecular Chaperones
  • PapD protein, E coli
  • PapG protein, E coli
  • Periplasmic Proteins
  • Fimbriae Proteins