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| <StructureSection load='2ifo' size='340' side='right'caption='[[2ifo]]' scene=''> | | <StructureSection load='2ifo' size='340' side='right'caption='[[2ifo]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[2ifo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Filamentous_bacteriophage Filamentous bacteriophage]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IFO FirstGlance]. <br> | | <table><tr><td colspan='2'>[[2ifo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Filamentous_phage Filamentous phage]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IFO FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ifd|1ifd]], [[1ifm|1ifm]], [[2ifm|2ifm]], [[3ifm|3ifm]], [[4ifm|4ifm]], [[1ifi|1ifi]], [[1ifj|1ifj]], [[1ifk|1ifk]], [[1ifl|1ifl]], [[1ifn|1ifn]]</div></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Fiber diffraction</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=2ifo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ifo OCA], [https://pdbe.org/2ifo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ifo RCSB], [https://www.ebi.ac.uk/pdbsum/2ifo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ifo ProSAT]</span></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=2ifo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ifo OCA], [https://pdbe.org/2ifo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ifo RCSB], [https://www.ebi.ac.uk/pdbsum/2ifo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ifo ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[https://www.uniprot.org/uniprot/CAPSD_BPXF CAPSD_BPXF]] 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).
| | [https://www.uniprot.org/uniprot/CAPSD_BPXF CAPSD_BPXF] 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;">
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| == Publication Abstract from PubMed ==
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| Inovirus (filamentous bacteriophage) is a simple system for studying the rules by which protein primary structure (amino acid sequence) controls secondary and higher order structure, and thereby function. The virus occurs naturally as a number of different strains with similar secondary and higher order structure, but the protein subunit that assembles to form the virion coat has quite different primary structures in different virus strains. Despite these differences in primary structure, the subunits of all strains have much the same size, about 50 residues, which are distributed by type in much the same way into three domains of primary structure: a collection of acidic residues in the N-terminal region, a hydrophobic domain of about 19 residues near the middle, and a collection of basic residues near the C-terminus. Each subunit can be closely approximated by an alpha-helix with its long axis roughly parallel to the fibre axis, sloping from large to small radius in the virion and interleaving between subunits in the next turn or level. The acidic residues near the N-terminus of the subunit face outwards on the virion surface, and explain the low isoelectric point of the virion; the basic residues near the C-terminus face inwards, where they neutralize the charge on the DNA at the core of the virion; and the hydrophobic central domain is involved in interactions which bind neighbouring subunits. Detailed X-ray fibre diffraction analysis of one strain gives the subunit structure. Comparative model-building studies of different strains illustrate the common structural principles.
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| Model-building studies of Inovirus: genetic variations on a geometric theme.,Marvin DA Int J Biol Macromol. 1990 Apr;12(2):125-38. PMID:2078529<ref>PMID:2078529</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 2ifo" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Filamentous bacteriophage]] | | [[Category: Filamentous phage]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Marvin, D A]] | | [[Category: Marvin DA]] |
| [[Category: Helical virus]]
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| [[Category: Virus]]
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