1zn5: Difference between revisions
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< | ==Solid State NMR Structure of the low-temperature form of the Pf1 Major Coat Protein in Magnetically Aligned Bacteriophage== | ||
<StructureSection load='1zn5' size='340' side='right'caption='[[1zn5]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1zn5]] 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=1ZN5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZN5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</td></tr> | |||
-- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zn5 OCA], [https://pdbe.org/1zn5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zn5 RCSB], [https://www.ebi.ac.uk/pdbsum/1zn5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zn5 ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[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). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The filamentous bacteriophage Pf1 undergoes a reversible temperature-dependent transition that is also influenced by salt concentrations. This structural responsiveness may be a manifestation of the important biological property of flexibility, which is necessary for long, thin filamentous assemblies as a protection against shear forces. To investigate structural changes in the major coat protein, one- and two-dimensional solid-state NMR spectra of concentrated solutions of Pf1 bacteriophage were acquired, and the structure of the coat protein determined at 0 degrees C was compared with the structure previously determined at 30 degrees C. Despite dramatic differences in the NMR spectra, the overall change in the coat protein structure is small. Changes in the orientation of the C-terminal helical segment and the conformation of the first five residues at the N-terminus are apparent. These results are consistent with prior studies by X-ray fiber diffraction and other biophysical methods. | |||
Structural basis of the temperature transition of Pf1 bacteriophage.,Thiriot DS, Nevzorov AA, Opella SJ Protein Sci. 2005 Apr;14(4):1064-70. Epub 2005 Mar 1. PMID:15741342<ref>PMID:15741342</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1zn5" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: Pseudomonas virus Pf1]] | |||
[[Category: Nevzorov AA]] | |||
== | [[Category: Opella SJ]] | ||
[[Category: Thiriot DS]] | |||
[[Category: | |||
[[Category: | |||
[[Category: Nevzorov | |||
[[Category: Opella | |||
[[Category: Thiriot | |||
Latest revision as of 12:20, 22 May 2024
Solid State NMR Structure of the low-temperature form of the Pf1 Major Coat Protein in Magnetically Aligned BacteriophageSolid State NMR Structure of the low-temperature form of the Pf1 Major Coat Protein in Magnetically Aligned Bacteriophage
Structural highlights
FunctionCAPSD_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). Publication Abstract from PubMedThe filamentous bacteriophage Pf1 undergoes a reversible temperature-dependent transition that is also influenced by salt concentrations. This structural responsiveness may be a manifestation of the important biological property of flexibility, which is necessary for long, thin filamentous assemblies as a protection against shear forces. To investigate structural changes in the major coat protein, one- and two-dimensional solid-state NMR spectra of concentrated solutions of Pf1 bacteriophage were acquired, and the structure of the coat protein determined at 0 degrees C was compared with the structure previously determined at 30 degrees C. Despite dramatic differences in the NMR spectra, the overall change in the coat protein structure is small. Changes in the orientation of the C-terminal helical segment and the conformation of the first five residues at the N-terminus are apparent. These results are consistent with prior studies by X-ray fiber diffraction and other biophysical methods. Structural basis of the temperature transition of Pf1 bacteriophage.,Thiriot DS, Nevzorov AA, Opella SJ Protein Sci. 2005 Apr;14(4):1064-70. Epub 2005 Mar 1. PMID:15741342[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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