Determination of solid-state NMR structures of proteins by means of three-dimensional 15N-13C-13C dipolar correlation spectroscopy and chemical shift analysis
- PMID: 14516199
- DOI: 10.1021/bi034903r
Determination of solid-state NMR structures of proteins by means of three-dimensional 15N-13C-13C dipolar correlation spectroscopy and chemical shift analysis
Abstract
In this paper, a three-dimensional (3D) NMR-based approach for the determination of the fold of moderately sized proteins by solid-state magic-angle spinning (MAS) NMR is presented and applied to the alpha-spectrin SH3 domain. This methodology includes the measurement of multiple (13)C-(13)C distance restraints on biosynthetically site-directed (13)C-enriched samples, obtained by growing bacteria on [2-(13)C]glycerol and [1,3-(13)C]glycerol. 3D (15)N-(13)C-(13)C dipolar correlation experiments were applied to resolve overlap of signals, in particular in the region where backbone carbon-carbon correlations of the C(alpha)-C(alpha), CO-CO, C(alpha)-CO, and CO-C(alpha) type appear. Additional restraints for confining the structure were obtained from phi and psi backbone torsion angles of 29 residues derived from C(alpha), C(beta), CO, NH, and H(alpha) chemical shifts. Using both distance and angular restraints, a refined structure was calculated with a backbone root-mean-square deviation of 0.7 A with respect to the average structure.
Similar articles
-
Measurement of multiple psi torsion angles in uniformly 13C,15N-labeled alpha-spectrin SH3 domain using 3D 15N-13C-13C-15N MAS dipolar-chemical shift correlation spectroscopy.J Am Chem Soc. 2003 Jun 4;125(22):6827-33. doi: 10.1021/ja029082c. J Am Chem Soc. 2003. PMID: 12769594
-
Determinations of 15N chemical shift anisotropy magnitudes in a uniformly 15N,13C-labeled microcrystalline protein by three-dimensional magic-angle spinning nuclear magnetic resonance spectroscopy.J Phys Chem B. 2006 Jun 8;110(22):10926-36. doi: 10.1021/jp060507h. J Phys Chem B. 2006. PMID: 16771346
-
Protein structure determination by high-resolution solid-state NMR spectroscopy: application to microcrystalline ubiquitin.J Am Chem Soc. 2005 Jun 22;127(24):8618-26. doi: 10.1021/ja0503128. J Am Chem Soc. 2005. PMID: 15954766
-
Solid-state nuclear magnetic resonance structural studies of proteins using paramagnetic probes.Solid State Nucl Magn Reson. 2012 May-Jun;43-44:1-13. doi: 10.1016/j.ssnmr.2012.02.007. Epub 2012 Mar 9. Solid State Nucl Magn Reson. 2012. PMID: 22464402 Review.
-
High-resolution solid-state MAS NMR of proteins-Crh as an example.Magn Reson Chem. 2007 Dec;45 Suppl 1:S24-31. doi: 10.1002/mrc.2106. Epub 2007 Dec 17. Magn Reson Chem. 2007. PMID: 18081212 Review.
Cited by
-
Assignment and secondary structure of the YadA membrane protein by solid-state MAS NMR.Sci Rep. 2012;2:803. doi: 10.1038/srep00803. Epub 2012 Nov 12. Sci Rep. 2012. PMID: 23150774 Free PMC article.
-
Partial 13C isotopic enrichment of nucleoside monophosphates: useful reporters for NMR structural studies.Nucleic Acids Res. 2005 Oct 27;33(18):e164. doi: 10.1093/nar/gni165. Nucleic Acids Res. 2005. PMID: 16254075 Free PMC article.
-
Peptide and Protein Dynamics and Low-Temperature/DNP Magic Angle Spinning NMR.J Phys Chem B. 2017 May 18;121(19):4997-5006. doi: 10.1021/acs.jpcb.7b02066. Epub 2017 May 10. J Phys Chem B. 2017. PMID: 28437077 Free PMC article.
-
Structural characterization of supramolecular assemblies by ¹³C spin dilution and 3D solid-state NMR.J Biomol NMR. 2013 Jan;55(1):1-9. doi: 10.1007/s10858-012-9691-9. Epub 2012 Dec 1. J Biomol NMR. 2013. PMID: 23202987
-
Dipole tensor-based atomic-resolution structure determination of a nanocrystalline protein by solid-state NMR.Proc Natl Acad Sci U S A. 2008 Mar 25;105(12):4621-6. doi: 10.1073/pnas.0712393105. Epub 2008 Mar 14. Proc Natl Acad Sci U S A. 2008. PMID: 18344321 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
