5JZR

Solid-state MAS NMR structure of Acinetobacter phage 205 (AP205) coat protein in assembled capsid particles

Summary for 5JZR

• Entry DOI: 10.2210/pdb5jzr/pdb
• NMR Information: BMRB: 30094
• Descriptor: Coat protein (1 entity in total)
• Functional Keywords: coat protein, viral protein
• Biological source: Acinetobacter phage AP205
• Total number of polymer chains: 2
• Total formula weight: 28045.68

Authors

Jaudzems, K.,Andreas, L.B.,Stanek, J.,Lalli, D.,Bertarello, A.,Le Marchand, T.,Cala-De Paepe, D.,Kotelovica, S.,Akopjana, I.,Knott, B.,Wegner, S.,Engelke, F.,Lesage, A.,Emsley, L.,Tars, K.,Herrmann, T.,Pintacuda, G. (deposition date: 2016-05-17, release date: 2016-08-10, Last modification date: 2024-06-19)

Primary citation

Andreas, L.B.,Jaudzems, K.,Stanek, J.,Lalli, D.,Bertarello, A.,Le Marchand, T.,Cala-De Paepe, D.,Kotelovica, S.,Akopjana, I.,Knott, B.,Wegner, S.,Engelke, F.,Lesage, A.,Emsley, L.,Tars, K.,Herrmann, T.,Pintacuda, G.
Structure of fully protonated proteins by proton-detected magic-angle spinning NMR.
Proc.Natl.Acad.Sci.USA, 113:9187-9192, 2016

PubMed Abstract: Protein structure determination by proton-detected magic-angle spinning (MAS) NMR has focused on highly deuterated samples, in which only a small number of protons are introduced and observation of signals from side chains is extremely limited. Here, we show in two fully protonated proteins that, at 100-kHz MAS and above, spectral resolution is high enough to detect resolved correlations from amide and side-chain protons of all residue types, and to reliably measure a dense network of (1)H-(1)H proximities that define a protein structure. The high data quality allowed the correct identification of internuclear distance restraints encoded in 3D spectra with automated data analysis, resulting in accurate, unbiased, and fast structure determination. Additionally, we find that narrower proton resonance lines, longer coherence lifetimes, and improved magnetization transfer offset the reduced sample size at 100-kHz spinning and above. Less than 2 weeks of experiment time and a single 0.5-mg sample was sufficient for the acquisition of all data necessary for backbone and side-chain resonance assignment and unsupervised structure determination. We expect the technique to pave the way for atomic-resolution structure analysis applicable to a wide range of proteins.

PubMed: 27489348
DOI: 10.1073/pnas.1602248113

Experimental method

SOLID-STATE NMR