Transferred nuclear Overhauser effect spectroscopy study of a peptide from 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 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.
Walse
B
B
Physical Chemistry 2, Center for Chemistry and Chemical Engineering, Lund University, Sweden.
Kihlberg
J
J
Karlsson
K F
KF
Nilsson
M
M
Wahlund
K G
KG
Pinkner
J S
JS
Hultgren
S J
SJ
Drakenberg
T
T
D018830:Adhesins, Escherichia coli / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D003460:Crystallization; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D018832:Molecular Chaperones; D015394:Molecular Structure; D033903:Periplasmic Proteins; D011487:Protein Conformation
D018830:Adhesins, Escherichia coli; D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; C084330:PapD protein, E coli; C092426:PapG protein, E coli; D033903:Periplasmic Proteins; D036781:Fimbriae Proteins