Related ArticlesThe NMR-Rosetta capsid model of M13 bacteriophage reveals a quadrupled hydrophobic packing epitope.
Proc Natl Acad Sci U S A. 2015 Jan 27;112(4):971-6
Authors: Morag O, Sgourakis NG, Baker D, Goldbourt A
Abstract
Filamentous phage are elongated semiflexible ssDNA viruses that infect bacteria. The M13 phage, belonging to the family inoviridae, has a length of ~1 ?m and a diameter of ~7 nm. Here we present a structural model for the capsid of intact M13 bacteriophage using Rosetta model building guided by structure restraints obtained from magic-angle spinning solid-state NMR experimental data. The C5 subunit symmetry observed in fiber diffraction studies was enforced during model building. The structure consists of stacked pentamers with largely alpha helical subunits containing an N-terminal type II ?-turn; there is a rise of 16.6-16.7 Ĺ and a tilt of 36.1-36.6° between consecutive pentamers. The packing of the subunits is stabilized by a repeating hydrophobic stacking pocket; each subunit participates in four pockets by contributing different hydrophobic residues, which are spread along the subunit sequence. Our study provides, to our knowledge, the first magic-angle spinning NMR structure of an intact filamentous virus capsid and further demonstrates the strength of this technique as a method of choice to study noncrystalline, high-molecular-weight molecular assemblies.
The NMR-Rosetta capsid model of M13 bacteriophage [Biophysics and Computational Biology]
The NMR-Rosetta capsid model of M13 bacteriophage
Morag, O., Sgourakis, N. G., Baker, D., Goldbourt, A....
Date: 2015-01-27
Filamentous phage are elongated semiflexible ssDNA viruses that infect bacteria. The M13 phage, belonging to the family inoviridae, has a length of ~1 ?m and a diameter of ~7 nm. Here we present a structural model for the capsid of intact M13 bacteriophage using Rosetta model building guided by structure... Read More
PNAS:
Number: 4
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[NMR paper] NMR Spectroscopy Reveals that Polyglutamine Binding Peptide 1 Adopts a Preferred Conformation with a Defined Hydrophobic Cluster.
NMR Spectroscopy Reveals that Polyglutamine Binding Peptide 1 Adopts a Preferred Conformation with a Defined Hydrophobic Cluster.
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Arch Biochem Biophys. 2014 Jul 4;
Authors: Ramos-Martín F, Hervás R, Vázquez MC, Laurents DV
Abstract
Several important human inherited neurodegenerative diseases are caused by "polyQ expansions", which are aberrant long repeats of glutamine residues in...
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Magic AngleSpinning NMR Reveals Sequence-DependentStructural Plasticity, Dynamics, and the Spacer Peptide 1 Conformationin HIV-1 Capsid Protein Assemblies
Magic AngleSpinning NMR Reveals Sequence-DependentStructural Plasticity, Dynamics, and the Spacer Peptide 1 Conformationin HIV-1 Capsid Protein Assemblies
Yun Han, Guangjin Hou, Christopher L. Suiter, Jinwoo Ahn, In-Ja L. Byeon, Andrew S. Lipton, Sarah Burton, Ivan Hung, Peter L. Gor?kov, Zhehong Gan, William Brey, David Rice, Angela M. Gronenborn and Tatyana Polenova
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja406907h/aop/images/medium/ja-2013-06907h_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja406907h...
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[NMR paper] Magic Angle Spinning NMR Reveals Sequence-Dependent Structural Plasticity, Dynamics, and the Spacer Peptide 1 Conformation in HIV-1 Capsid Protein Assemblies.
Magic Angle Spinning NMR Reveals Sequence-Dependent Structural Plasticity, Dynamics, and the Spacer Peptide 1 Conformation in HIV-1 Capsid Protein Assemblies.
Magic Angle Spinning NMR Reveals Sequence-Dependent Structural Plasticity, Dynamics, and the Spacer Peptide 1 Conformation in HIV-1 Capsid Protein Assemblies.
J Am Chem Soc. 2013 Oct 28;
Authors: Han Y, Hou G, Suiter CL, Ahn J, Byeon IJ, Lipton AS, Burton SD, Hung I, Gor'kov PL, Gan Z, Brey WW, Rice D, Gronenborn AM, Polenova TE
Abstract
A key stage in HIV-1 maturation towards...
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[NMR paper] Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
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J Am Chem Soc. 2005 Aug 24;127(33):11676-83
Authors: Desvaux H, Dubois L, Huber G, Quillin ML, Berthault P, Matthews BW
Wild-type bacteriophage T4 lysozyme contains a hydrophobic cavity with binding properties that have been...
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[NMR paper] NMR solution structure of the monomeric form of the bacteriophage lambda capsid stabi
NMR solution structure of the monomeric form of the bacteriophage lambda capsid stabilizing protein gpD.
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J Biomol NMR. 2005 Apr;31(4):351-6
Authors: Iwai H, Forrer P, Plückthun A, Güntert P
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[NMR paper] NMR analysis reveals a positively charged hydrophobic domain as a common motif to bou
NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
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Biochemistry. 1994 Jan 25;33(3):644-50
Authors: Fraenkel Y, Gershoni JM, Navon G
A complete 1H assignment of d-tubocurarine was carried out using 1D and 2D NMR techniques. Geometries of free acetylcholine (ACh) and d-tubocurarine were compared with those of the ligands bound to a...
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[NMR paper] NMR analysis reveals a positively charged hydrophobic domain as a common motif to bou
NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
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Biochemistry. 1994 Jan 25;33(3):644-50
Authors: Fraenkel Y, Gershoni JM, Navon G
A complete 1H assignment of d-tubocurarine was carried out using 1D and 2D NMR techniques. Geometries of free acetylcholine (ACh) and d-tubocurarine were compared with those of the ligands bound to a...