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Title: Bacteriophage Tail-Tube Assembly Studied by Proton-Detected 4D Solid-State NMR

Journal Article · · Angewandte Chemie (International Edition)
 [1];  [2];  [3];  [2];  [4];  [2];  [3]; ORCiD logo [5]
  1. Leibniz-Forschungsinstitut fur Molekulare Pharmakologie (FMP), Berlin (Germany). Department of Molecular Biophysics
  2. Leibniz-Forschungsinstitut fur Molekulare Pharmakologie (FMP), Berlin (Germany). Department of Molecular Biophysics
  3. University of Paris-Sud, University of Paris-Saclay (France). Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS
  4. Brookhaven National Lab. (BNL), Upton, NY (United States)
  5. Leibniz-Forschungsinstitut fur Molekulare Pharmakologie (FMP), Berlin (Germany). Department of Molecular Biophysics; Humboldt Univ. of Berlin (Germany). Institute of Biology
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Obtaining unambiguous resonance assignments remains a major bottleneck in solid-state NMR studies of protein structure and dynamics. Particularly for supramolecular assemblies with large subunits (>150 residues), the analysis of crowded spectral data presents a challenge, even if three-dimensional (3D) spectra are used. Here, we present a proton-detected 4D solid-state NMR assignment procedure that is tailored for large assemblies. The key to recording 4D spectra with three indirect carbon or nitrogen dimensions with their inherently large chemical shift dispersion lies in the use of sparse non-uniform sampling (as low as 2 %). As a proof of principle, we acquired 4D (H)COCANH, (H)CACONH, and (H)CBCANH spectra of the 20 kDa bacteriophage tail-tube protein gp17.1 in a total time of two and a half weeks. These spectra were sufficient to obtain complete resonance assignments in a straightforward manner without use of previous solution NMR data.

Research Organization:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER)
Grant/Contract Number:
SC0012704
OSTI ID:
1376150
Report Number(s):
BNL-114099-2017-JA
Journal Information:
Angewandte Chemie (International Edition), Vol. 56, Issue 32; ISSN 1433-7851
Publisher:
WileyCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 18 works
Citation information provided by
Web of Science

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Cited By (6)

Non-uniform sampling in quantitative assessment of heterogeneous solid-state NMR line shapes journal December 2019
Assessment of Non‐Uniform Sampling Schemes in Solid State NMR of Bacteriophage Viruses journal August 2019
Assessment of a Large Enzyme–Drug Complex by Proton‐Detected Solid‐State NMR Spectroscopy without Deuteration journal February 2019
Automated projection spectroscopy in solid-state NMR journal November 2018
Structure, function and assembly of the long, flexible tail of siphophages journal December 2020
Charakterisierung eines großen Enzym‐Wirkstoff‐Komplexes mittels protonendetektierter Festkörper‐NMR ohne Deuterierung journal February 2019

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
bacteriophage
gp17.1
non-uniform sampling
protein structures
solid-state NMR