NDLI: Encoded loop-lanthanide-binding tags for long-range distance measurements in proteins by NMR and EPR spectroscopy

Content Provider	Springer Nature Link
Author	Barthelmes, Dominic Gränz, Markus Barthelmes, Katja Allen, Karen N. Imperiali, Barbara Prisner, Thomas Schwalbe, Harald
Copyright Year	2015
Abstract	We recently engineered encodable lanthanide binding tags (LBTs) into proteins and demonstrated their applicability in Nuclear Magnetic Resonance (NMR) spectroscopy, X-ray crystallography and luminescence studies. Here, we engineered two-loop-LBTs into the model protein interleukin-1β (IL1β) and measured $^{1}$H, $^{15}$N-pseudocontact shifts (PCSs) by NMR spectroscopy. We determined the Δχ-tensors associated with each Tm$^{3+}$-loaded loop-LBT and show that the experimental PCSs yield structural information at the interface between the two metal ion centers at atomic resolution. Such information is very valuable for the determination of the sites of interfaces in protein–protein-complexes. Combining the experimental PCSs of the two-loop-LBT construct IL1β-S2R2 and the respective single-loop-LBT constructs IL1β-S2, IL1β-R2 we additionally determined the distance between the metal ion centers. Further, we explore the use of two-loop LBTs loaded with Gd$^{3+}$ as a novel tool for distance determination by Electron Paramagnetic Resonance spectroscopy and show the NMR-derived distances to be remarkably consistent with distances derived from Pulsed Electron–Electron Dipolar Resonance.
Starting Page	275
Ending Page	282
Page Count	8
File Format	PDF
ISSN	09252738
Journal	Journal of Biomolecular NMR
Volume Number	63
Issue Number	3
e-ISSN	15735001
Language	English
Publisher	Springer Netherlands
Publisher Date	2015-09-04
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Paramagnetic NMR EPR PELDOR Lanthanide binding tags Biophysics and Biological Physics Biochemistry Spectroscopy/Spectrometry
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Biochemistry

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