PMID:9257702
| Citation |
Walse, B, Kihlberg, J, Karlsson, KF, Nilsson, M, Wahlund, KG, Pinkner, JS, Hultgren, SJ and Drakenberg, T (1997) Transferred nuclear Overhauser effect spectroscopy study of a peptide from the PapG pilus subunit bound by the Escherichia coli PapD chaperone. FEBS Lett. 412:115-20 |
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| 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. |
| Links | |
| Keywords |
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 |
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