Secondary structure of filamentous bacteriophage coat protein is preserved in lipid environments

Schiksnis, Robert A.; Bogusky, Michael J.; Opella, Stanley J.

doi:10.1016/0022-2836(88)90485-8

Cited by 12 publications

(13 citation statements)

References 11 publications

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“…They are consistent with the data from selectively 15 N-labeled samples as analyzed with the shotgun approach based on the periodicity of an a-helix observed in PISA wheels and Dipolar waves. However, it is also possible to implement structural fitting 21 in an "assignmentfree" manner, and this yielded a very similar structure with an RMSD value to the average of all the resulting structures of 1.6 Å .…”

supporting

confidence: 78%

“…17,18 All spectral features apparent in Figure 1(a) have been confirmed in spectra of uniformly 15 N-labeled samples obtained under slightly different experimental conditions, e.g. offset frequencies or radio frequency power levels, or in those of selectively 15 N-labeled samples, as shown in Figure 1(d). The resonance assignments were obtained with a modified version of the shotgun NMR approach applied to fd coat protein in lipid bilayers 22 and virus particles.…”

Section: Nmr Spectroscopy Of Pf1 Virus Particlesmentioning

confidence: 58%

“…20 This approach takes advantage of the scattering of each type of residue throughout the sequence and the symmetry inherent in helical structures. Nearly all (41 out of 46) of the residues in the protein are accounted for in the spectra of the nine selectively 15 N-labeled samples shown in Figure 1(d) and the spectrum of the selectively "unlabeled" sample shown in Figure 2(a). The polarity index slant angle (PISA) wheel 23,24 ( Figure 1(b) and (c)) and dipolar wave 25,26 ( Figure 3) patterns evident in the experimental data were analyzed iteratively, simultaneously assigning the resonances and determining an initial model of the structure.…”

Section: Nmr Spectroscopy Of Pf1 Virus Particlesmentioning

confidence: 99%

“…For uniformly 15 N-labeled bacteriophage, the minimal growth media was comprised of the following: 11 g/l Na 2 HPO 4 , 3 g/l KH 2 PO 4 , 0.5 g/l NaCl, 1 g/l MgSO 4 -7H 2 O, 0.025 g/l CaCl 2 -2H 2 O, 10 g/l dextrose, 0.1 g/l thiamine hydrochloride, 10 ml/l 100X MEM vitamin solution (Sigma, M6895), and 1 g/l […”

Section: Pf1 Sample Preparationmentioning

confidence: 99%

“…Comparisons of the structure and dynamics of Pf1 coat protein in membrane environments 12 -17 and in bacteriophage particles provide insights into the structural rearrangement that accompanies viral assembly. 15,18,19 As demonstrated with fd (PDB entry 1NH4), 20 the backbone structure of the coat protein in a filamentous bacteriophage particle can be determined from the orientational constraints provided by the 15 N chemical shift and 1 …”

Section: Introductionmentioning

confidence: 99%

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Structure of the Coat Protein in Pf1 Bacteriophage Determined by Solid-state NMR Spectroscopy

Thiriot

Nevzorov

Zagyanskiy

et al. 2004

Journal of Molecular Biology

134

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The atomic resolution structure of Pf1 coat protein determined by solidstate NMR spectroscopy of magnetically aligned filamentous bacteriophage particles in solution is compared to the structures previously determined by X-ray fiber and neutron diffraction, the structure of its membrane-bound form, and the structure of fd coat protein. These structural comparisons provide insights into several biological properties, differences between class I and class II filamentous bacteriophages, and the assembly process. The six N-terminal amino acid residues adopt an unusual "double hook" conformation on the outside of the bacteriophage particle. The solid-state NMR results indicate that at 30 8C, some of the coat protein subunits assume a single, fully structured conformation, and some have a few mobile residues that provide a break between two helical segments, in agreement with structural models from X-ray fiber and neutron diffraction, respectively. The atomic resolution structure determined by solid-state NMR for residues 7 -14 and 18 -46, which excludes the N-terminal double hook and the break between the helical segments, but encompasses more than 80% of the backbone including the distinct kink at residue 29, agrees with that determined by X-ray fiber diffraction with an RMSD value of 2.0 Å . The symmetry and distance constraints determined by X-ray fiber and neutron diffraction enable the construction of an accurate model of the bacteriophage particle from the coordinates of the coat protein monomers.

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supporting

confidence: 78%

Section: Nmr Spectroscopy Of Pf1 Virus Particlesmentioning

confidence: 58%

Section: Nmr Spectroscopy Of Pf1 Virus Particlesmentioning

confidence: 99%

Section: Pf1 Sample Preparationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Structure of the Coat Protein in Pf1 Bacteriophage Determined by Solid-state NMR Spectroscopy

Thiriot

Nevzorov

Zagyanskiy

et al. 2004

Journal of Molecular Biology

134

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Comparison of the dynamics of the membrane‐bound form of fd coat protein in micelles and in bilayers by solution and solid‐state nitrogen‐15 nuclear magnetic resonance spectroscopy

1988

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Solid-state and solution 15N nuclear magnetic resonance experiments on uniformly and specifically 15N labeled coat protein in phospholipid bilayers and in detergent micelles are used to describe the dynamics of the membrane-bound form of the protein. The residues in the N- and C-terminal portions of the coat protein in both phospholipid bilayers and in detergent micelles are mobile, while those in the hydrophobic midsection are immobile. There is evidence for a gradient of mobility in the C-terminal region of the coat protein in micelles; at 25 degrees C only the last two residues are mobile on the 10(9)-Hz timescale, while the last six to eight residues appear to be mobile on slower timescales and highly mobile at higher temperatures. Since all of the C-terminal residues are immobile in the virus particles, the mobility of these residues in the membrane-bound form of the protein may be important for the formation of protein-DNA interactions in the assembly process.

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Detergent-solubilized M13 coat protein exists as an asymmetric dimer

Henry

Sykes

1990

Journal of Molecular Biology

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Secondary structure of filamentous bacteriophage coat protein is preserved in lipid environments

Cited by 12 publications

References 11 publications

Structure of the Coat Protein in Pf1 Bacteriophage Determined by Solid-state NMR Spectroscopy

Structure of the Coat Protein in Pf1 Bacteriophage Determined by Solid-state NMR Spectroscopy

Comparison of the dynamics of the membrane‐bound form of fd coat protein in micelles and in bilayers by solution and solid‐state nitrogen‐15 nuclear magnetic resonance spectroscopy

Detergent-solubilized M13 coat protein exists as an asymmetric dimer

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