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

Björn Walse; Jan Kihlberg; Katarina Flemmer Karlsson; Mikael Nilsson; Karl Gustav Wahlund; Jerome S. Pinkner; Scott J. Hultgren; Torbjörn Drakenberg

doi:10.1016/S0014-5793(97)00759-X

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

Björn Walse
, Jan Kihlberg
, Katarina Flemmer Karlsson
, Mikael Nilsson
, Karl Gustav Wahlund
, Jerome S. Pinkner
, Scott J. Hultgren
, Torbjörn Drakenberg

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

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(α)H/NH and C(β)H/NH TRNOEs and the absence of sequential NH(i)/NH(i+1) TROEs 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.

Original language	English
Pages (from-to)	115-120
Number of pages	6
Journal	FEBS Letters
Volume	412
Issue number	1
DOIs	https://doi.org/10.1016/S0014-5793(97)00759-X
State	Published - Jul 21 1997

Keywords

NMR
P pili
PapD chaperone
Protein-peptide interaction
Transferred NOE

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10.1016/S0014-5793(97)00759-X

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@article{b65d2f99c07c4ce7940028c837001730,

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

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(α)H/NH and C(β)H/NH TRNOEs and the absence of sequential NH(i)/NH(i+1) TROEs 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.",

keywords = "NMR, P pili, PapD chaperone, Protein-peptide interaction, Transferred NOE",

author = "Bj{\"o}rn Walse and Jan Kihlberg and \{Flemmer Karlsson\}, Katarina and Mikael Nilsson and Wahlund, \{Karl Gustav\} and Pinkner, \{Jerome S.\} and Hultgren, \{Scott J.\} and Torbj{\"o}rn Drakenberg",

note = "Funding Information: The authors would like to thank G. Soto for providing the dissociation constant of the modified PapG307-314 peptide, S. Linse for the generous gift of Calbindin D 28k and G. Carlstr{\"o}m for pulse sequence programming. This work was funded by the Swedish National Board for Industrial and Technical Development (NUTEK) and by the Swedish Natural Science Research Council (NFR).",

year = "1997",

month = jul,

day = "21",

doi = "10.1016/S0014-5793(97)00759-X",

language = "English",

volume = "412",

pages = "115--120",

journal = "FEBS Letters",

issn = "0014-5793",

number = "1",

}

TY - JOUR

T1 - Transferred nuclear Overhauser effect spectroscopy study of a peptide from the PapG pilus subunit bound by the Escherichia coli PapD chaperone

AU - Walse, Björn

AU - Kihlberg, Jan

AU - Flemmer Karlsson, Katarina

AU - Nilsson, Mikael

AU - Wahlund, Karl Gustav

AU - Pinkner, Jerome S.

AU - Hultgren, Scott J.

AU - Drakenberg, Torbjörn

N1 - Funding Information: The authors would like to thank G. Soto for providing the dissociation constant of the modified PapG307-314 peptide, S. Linse for the generous gift of Calbindin D 28k and G. Carlström for pulse sequence programming. This work was funded by the Swedish National Board for Industrial and Technical Development (NUTEK) and by the Swedish Natural Science Research Council (NFR).

PY - 1997/7/21

Y1 - 1997/7/21

N2 - 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(α)H/NH and C(β)H/NH TRNOEs and the absence of sequential NH(i)/NH(i+1) TROEs 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.

AB - 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(α)H/NH and C(β)H/NH TRNOEs and the absence of sequential NH(i)/NH(i+1) TROEs 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.

KW - NMR

KW - P pili

KW - PapD chaperone

KW - Protein-peptide interaction

KW - Transferred NOE

UR - https://www.scopus.com/pages/publications/0030872740

U2 - 10.1016/S0014-5793(97)00759-X

DO - 10.1016/S0014-5793(97)00759-X

M3 - Article

C2 - 9257702

AN - SCOPUS:0030872740

SN - 0014-5793

VL - 412

SP - 115

EP - 120

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

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

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Keywords

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