1pjf
From Proteopedia
(New page: 200px<br /><applet load="1pjf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pjf" /> '''Solid State NMR structure of the Pf1 Major C...) |
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'''Solid State NMR structure of the Pf1 Major Coat Protein in Magnetically Aligned Bacteriophage'''<br /> | '''Solid State NMR structure of the Pf1 Major Coat Protein in Magnetically Aligned Bacteriophage'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The atomic resolution structure of Pf1 coat protein determined by | + | The atomic resolution structure of Pf1 coat protein determined by solid-state 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 degrees C, 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 A. 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1PJF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_phage_pf1 Pseudomonas phage pf1]. Full crystallographic information is available from [http:// | + | 1PJF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_phage_pf1 Pseudomonas phage pf1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PJF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pseudomonas phage pf1]] | [[Category: Pseudomonas phage pf1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Nevzorov, A | + | [[Category: Nevzorov, A A.]] |
| - | [[Category: Opella, S | + | [[Category: Opella, S J.]] |
| - | [[Category: Thiriot, D | + | [[Category: Thiriot, D S.]] |
| - | [[Category: Wu, C | + | [[Category: Wu, C H.]] |
[[Category: Zagyanskiy, L.]] | [[Category: Zagyanskiy, L.]] | ||
[[Category: helical virus]] | [[Category: helical virus]] | ||
[[Category: virus/viral protein]] | [[Category: virus/viral protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:25 2008'' |
Revision as of 12:29, 21 February 2008
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Solid State NMR structure of the Pf1 Major Coat Protein in Magnetically Aligned Bacteriophage
Overview
The atomic resolution structure of Pf1 coat protein determined by solid-state 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 degrees C, 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 A. 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.
About this Structure
1PJF is a Single protein structure of sequence from Pseudomonas phage pf1. Full crystallographic information is available from OCA.
Reference
Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy., Thiriot DS, Nevzorov AA, Zagyanskiy L, Wu CH, Opella SJ, J Mol Biol. 2004 Aug 13;341(3):869-79. PMID:15288792
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