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2ksj

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==Structure and Dynamics of the Membrane-bound form of Pf1 Coat Protein: Implications for Structural Rearrangement During Virus Assembly==
==Structure and Dynamics of the Membrane-bound form of Pf1 Coat Protein: Implications for Structural Rearrangement During Virus Assembly==
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<StructureSection load='2ksj' size='340' side='right' caption='[[2ksj]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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<StructureSection load='2ksj' size='340' side='right'caption='[[2ksj]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ksj]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KSJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KSJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ksj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_virus_Pf1 Pseudomonas virus Pf1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KSJ FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ksj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ksj OCA], [http://pdbe.org/2ksj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ksj RCSB], [http://www.ebi.ac.uk/pdbsum/2ksj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ksj ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Hybrid , Solid-state NMR , Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ksj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ksj OCA], [https://pdbe.org/2ksj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ksj RCSB], [https://www.ebi.ac.uk/pdbsum/2ksj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ksj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CAPSD_BPPF1 CAPSD_BPPF1]] Self assembles to form a helical capsid wrapping up the viral genomic DNA. The capsid displays a filamentous structure with a length of 760-1950 nm and a width of 6-8 nm. The virion assembly and budding take place at the host inner membrane (By similarity).
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[https://www.uniprot.org/uniprot/CAPSD_BPPF1 CAPSD_BPPF1] Self assembles to form a helical capsid wrapping up the viral genomic DNA. The capsid displays a filamentous structure with a length of 760-1950 nm and a width of 6-8 nm. The virion assembly and budding take place at the host inner membrane (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The three-dimensional structure of the membrane-bound form of the major coat protein of Pf1 bacteriophage was determined in phospholipid bilayers using orientation restraints derived from both solid-state and solution NMR experiments. In contrast to previous structures determined solely in detergent micelles, the structure in bilayers contains information about the spatial arrangement of the protein within the membrane, and thus provides insights to the bacteriophage assembly process from membrane-inserted to bacteriophage-associated protein. Comparisons between the membrane-bound form of the coat protein and the previously determined structural form found in filamentous bacteriophage particles demonstrate that it undergoes a significant structural rearrangement during the membrane-mediated virus assembly process. The rotation of the transmembrane helix (Q16-A46) around its long axis changes dramatically (by 160 degrees) to obtain the proper alignment for packing in the virus particles. Furthermore, the N-terminal amphipathic helix (V2-G17) tilts away from the membrane surface and becomes parallel with the transmembrane helix to form one nearly continuous long helix. The spectra obtained in glass-aligned planar lipid bilayers, magnetically aligned lipid bilayers (bicelles), and isotropic lipid bicelles reflect the effects of backbone motions and enable the backbone dynamics of the N-terminal helix to be characterized. Only resonances from the mobile N-terminal helix and the C-terminus (A46) are observed in the solution NMR spectra of the protein in isotropic q &gt; 1 bicelles, whereas only resonances from the immobile transmembrane helix are observed in the solid-state (1)H/(15)N-separated local field spectra in magnetically aligned bicelles. The N-terminal helix and the hinge that connects it to the transmembrane helix are significantly more dynamic than the rest of the protein, thus facilitating structural rearrangement during bacteriophage assembly.
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Structure and dynamics of the membrane-bound form of Pf1 coat protein: implications of structural rearrangement for virus assembly.,Park SH, Marassi FM, Black D, Opella SJ Biophys J. 2010 Sep 8;99(5):1465-74. PMID:20816058<ref>PMID:20816058</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ksj" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Black, D]]
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[[Category: Large Structures]]
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[[Category: Marassi, F]]
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[[Category: Pseudomonas virus Pf1]]
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[[Category: Opella, S J]]
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[[Category: Black D]]
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[[Category: Park, S]]
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[[Category: Marassi F]]
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[[Category: Capsid protein]]
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[[Category: Opella SJ]]
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[[Category: Host membrane]]
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[[Category: Park S]]
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[[Category: Membrane]]
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[[Category: Membrane protein]]
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[[Category: Transmembrane]]
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[[Category: Viral protein]]
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[[Category: Virion]]
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Current revision

Structure and Dynamics of the Membrane-bound form of Pf1 Coat Protein: Implications for Structural Rearrangement During Virus Assembly

PDB ID 2ksj

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