1nh4: Difference between revisions
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==Structure of the coat protein in fd filamentous bacteriophage particles== | |||
<StructureSection load='1nh4' size='340' side='right'caption='[[1nh4]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1nh4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_fd Enterobacteria phage fd]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NH4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NH4 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=1nh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nh4 OCA], [https://pdbe.org/1nh4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nh4 RCSB], [https://www.ebi.ac.uk/pdbsum/1nh4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nh4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CAPSD_BPFD CAPSD_BPFD] 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 atomic resolution structure of fd coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles differs from that previously determined by x-ray fiber diffraction. Most notably, the 50-residue protein is not a single curved helix, but rather is a nearly ideal straight helix between residues 7 and 38, where there is a distinct kink, and then a straight helix with a different orientation between residues 39 and 49. Residues 1-5 have been shown to be mobile and unstructured, and proline 6 terminates the helix. The structure of the coat protein in virus particles, in combination with the structure of the membrane-bound form of the same protein in bilayers, also recently determined by solid-state NMR spectroscopy, provides insight into the viral assembly process. In addition to their roles in molecular biology and biotechnology, the filamentous bacteriophages continue to serve as model systems for the development of experimental methods for determining the structures of proteins in biological supramolecular assemblies. New NMR results include the complete sequential assignment of the two-dimensional polarization inversion spin-exchange at the magic angle spectrum of a uniformly 15N-labeled 50-residue protein in a 1.6 x 107 Da particle in solution, and the calculation of the three-dimensional structure of the protein from orientational restraints with an accuracy equivalent to an rms deviation of approximately 1A. | |||
Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy.,Zeri AC, Mesleh MF, Nevzorov AA, Opella SJ Proc Natl Acad Sci U S A. 2003 May 27;100(11):6458-63. Epub 2003 May 15. PMID:12750469<ref>PMID:12750469</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1nh4" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Enterobacteria phage fd]] | [[Category: Enterobacteria phage fd]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mesleh MF]] | ||
[[Category: | [[Category: Nevzorov AA]] | ||
[[Category: | [[Category: Opella SJ]] | ||
[[Category: | [[Category: Zeri AC]] | ||
Latest revision as of 11:54, 22 May 2024
Structure of the coat protein in fd filamentous bacteriophage particlesStructure of the coat protein in fd filamentous bacteriophage particles
Structural highlights
FunctionCAPSD_BPFD 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 atomic resolution structure of fd coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles differs from that previously determined by x-ray fiber diffraction. Most notably, the 50-residue protein is not a single curved helix, but rather is a nearly ideal straight helix between residues 7 and 38, where there is a distinct kink, and then a straight helix with a different orientation between residues 39 and 49. Residues 1-5 have been shown to be mobile and unstructured, and proline 6 terminates the helix. The structure of the coat protein in virus particles, in combination with the structure of the membrane-bound form of the same protein in bilayers, also recently determined by solid-state NMR spectroscopy, provides insight into the viral assembly process. In addition to their roles in molecular biology and biotechnology, the filamentous bacteriophages continue to serve as model systems for the development of experimental methods for determining the structures of proteins in biological supramolecular assemblies. New NMR results include the complete sequential assignment of the two-dimensional polarization inversion spin-exchange at the magic angle spectrum of a uniformly 15N-labeled 50-residue protein in a 1.6 x 107 Da particle in solution, and the calculation of the three-dimensional structure of the protein from orientational restraints with an accuracy equivalent to an rms deviation of approximately 1A. Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy.,Zeri AC, Mesleh MF, Nevzorov AA, Opella SJ Proc Natl Acad Sci U S A. 2003 May 27;100(11):6458-63. Epub 2003 May 15. PMID:12750469[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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