Analysis of influenza A virus NS1 dimer interfaces in solution by pulse EPR distance measurements

Philip S Kerry; Hannah L Turkington; Katrin Ackermann; Stephen A Jameison; Bela Ernest Bode

doi:10.1021/jp508386r

Analysis of influenza A virus NS1 dimer interfaces in solution by pulse EPR distance measurements

Philip S Kerry, Hannah L Turkington, Katrin Ackermann, Stephen A Jameison, Bela Ernest Bode

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

Abstract

Pulsed electron-electron double resonance (PELDOR) is an electron paramagnetic resonance (EPR) spectroscopy technique for nanometer distance measurements between paramagnetic centres such as radicals. PELDOR has been recognized as a valuable tool to approach structural questions in biological systems. In this manuscript we demonstrate the value of distance measurements for differentiating competing structural models on the dimerization of the effector domain (ED) of the non-structural protein 1 (NS1) of the influenza A virus. Our results show NS1 to be well amenable to nanometer distance measurements by EPR, yielding high quality data. In combination with mutants perturbing protein dimerization and in silico prediction based on crystal structures we can exclude one of two potential dimerization interfaces. Furthermore, our results lead to a viable hypothesis of a NS1 ED:ED interface which is flexible through rotation around the vector interconnecting the two native cysteines. These results prove the high value of pulse EPR as a complementary method for structural biology.

Original language	English
Pages (from-to)	10882-10888
Number of pages	7
Journal	Journal of Physical Chemistry B
Volume	118
Issue number	37
DOIs	https://doi.org/10.1021/jp508386r
Publication status	Published - 22 Aug 2014

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10.1021/jp508386r

Ackermann_2014_JPC_Analysis
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Oligo PELDOR: Oligo PELDOR
Bode, B. E. (PI)
European Commission
1/03/13 → 28/02/17
Project: Fellowship
State of the art pulse EPR instrumentati: State of the art pulse EPR instrumentation for long range distance measurements in biomacromolecules
Smith, G. M. (PI), Bode, B. E. (CoI), Naismith, J. (CoI), Schiemann, O. (CoI) & White, M. (CoI)
The Wellcome Trust
1/09/12 → 31/08/17
Project: Standard

Cite this

@article{abc901cc1da74b9da7b07347942071ea,

title = "Analysis of influenza A virus NS1 dimer interfaces in solution by pulse EPR distance measurements",

abstract = "Pulsed electron-electron double resonance (PELDOR) is an electron paramagnetic resonance (EPR) spectroscopy technique for nanometer distance measurements between paramagnetic centres such as radicals. PELDOR has been recognized as a valuable tool to approach structural questions in biological systems. In this manuscript we demonstrate the value of distance measurements for differentiating competing structural models on the dimerization of the effector domain (ED) of the non-structural protein 1 (NS1) of the influenza A virus. Our results show NS1 to be well amenable to nanometer distance measurements by EPR, yielding high quality data. In combination with mutants perturbing protein dimerization and in silico prediction based on crystal structures we can exclude one of two potential dimerization interfaces. Furthermore, our results lead to a viable hypothesis of a NS1 ED:ED interface which is flexible through rotation around the vector interconnecting the two native cysteines. These results prove the high value of pulse EPR as a complementary method for structural biology.",

author = "Kerry, {Philip S} and Turkington, {Hannah L} and Katrin Ackermann and Jameison, {Stephen A} and Bode, {Bela Ernest}",

note = "H.L.T. was supported by the University of St Andrews; S.A.J. is supported by the BBSRC, U.K.; P.S.K. is supported by the Medical Research Council, U.K.; B.E.B. is grateful for an EaStCHEM Hirst Academic Fellowship by the School of Chemistry, St Andrews, and funding from the People Programme (Marie Curie Actions) of the European Union{\textquoteright}s Seventh Framework Programme [REA 334496]. This work was supported by the Wellcome Trust [099149/Z/12/Z].",

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doi = "10.1021/jp508386r",

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T1 - Analysis of influenza A virus NS1 dimer interfaces in solution by pulse EPR distance measurements

AU - Kerry, Philip S

AU - Turkington, Hannah L

AU - Ackermann, Katrin

AU - Jameison, Stephen A

AU - Bode, Bela Ernest

N1 - H.L.T. was supported by the University of St Andrews; S.A.J. is supported by the BBSRC, U.K.; P.S.K. is supported by the Medical Research Council, U.K.; B.E.B. is grateful for an EaStCHEM Hirst Academic Fellowship by the School of Chemistry, St Andrews, and funding from the People Programme (Marie Curie Actions) of the European Union’s Seventh Framework Programme [REA 334496]. This work was supported by the Wellcome Trust [099149/Z/12/Z].

PY - 2014/8/22

Y1 - 2014/8/22

N2 - Pulsed electron-electron double resonance (PELDOR) is an electron paramagnetic resonance (EPR) spectroscopy technique for nanometer distance measurements between paramagnetic centres such as radicals. PELDOR has been recognized as a valuable tool to approach structural questions in biological systems. In this manuscript we demonstrate the value of distance measurements for differentiating competing structural models on the dimerization of the effector domain (ED) of the non-structural protein 1 (NS1) of the influenza A virus. Our results show NS1 to be well amenable to nanometer distance measurements by EPR, yielding high quality data. In combination with mutants perturbing protein dimerization and in silico prediction based on crystal structures we can exclude one of two potential dimerization interfaces. Furthermore, our results lead to a viable hypothesis of a NS1 ED:ED interface which is flexible through rotation around the vector interconnecting the two native cysteines. These results prove the high value of pulse EPR as a complementary method for structural biology.

AB - Pulsed electron-electron double resonance (PELDOR) is an electron paramagnetic resonance (EPR) spectroscopy technique for nanometer distance measurements between paramagnetic centres such as radicals. PELDOR has been recognized as a valuable tool to approach structural questions in biological systems. In this manuscript we demonstrate the value of distance measurements for differentiating competing structural models on the dimerization of the effector domain (ED) of the non-structural protein 1 (NS1) of the influenza A virus. Our results show NS1 to be well amenable to nanometer distance measurements by EPR, yielding high quality data. In combination with mutants perturbing protein dimerization and in silico prediction based on crystal structures we can exclude one of two potential dimerization interfaces. Furthermore, our results lead to a viable hypothesis of a NS1 ED:ED interface which is flexible through rotation around the vector interconnecting the two native cysteines. These results prove the high value of pulse EPR as a complementary method for structural biology.

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DO - 10.1021/jp508386r

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SP - 10882

EP - 10888

JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

IS - 37

ER -

Analysis of influenza A virus NS1 dimer interfaces in solution by pulse EPR distance measurements

Abstract

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Oligo PELDOR: Oligo PELDOR

State of the art pulse EPR instrumentati: State of the art pulse EPR instrumentation for long range distance measurements in biomacromolecules

Cite this